TY  - CONF
AU  - Jovanović, Zorana
AU  - Gligorijević, Nikola
AU  - Annighöfer, Burkhard
AU  - Dudzinski, Daniel
AU  - Nikolić, Milan
AU  - Pavlović, Vladimir
AU  - Lević, Steva
AU  - Brûlet, Annie
AU  - Assifaoui, Ali
AU  - Combet, Sophie
AU  - Minić, Simeon
PY  - 2024
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/7607
AB  - C-Phycocyanin (C-PC), the natural blue dye and the major protein in Spirulina, has high potential in the food industry due to its vivid colour and bioactive properties. However, low stability limits C-PC application potential, requiring approaches to strengthen its stability. Our study aimed to preserve C-PC by its incorporation into hydrogels formed by combining starch and β-lactoglobulin (BLG) using high-pressure (HP) processing. Notably, thermal treatment resulted in the complete loss of colour derived from C-PC. We performed a comprehensive characterization of the resulting HP gels by rheology measurements, texture profile analysis (TPA), small-angle X-ray scattering (SAXS), and scanning electron microscopy (SEM). Different compositions of binary (BLG/C-PC) and ternary (starch/BLG/C-PC) systems were processed under high-pressure (HP) conditions reaching up to 4,500 bar. The C-PC pigment was effectively preserved by mixing BLG and starch with C-PC at pH 7, maintaining concentrations of 180, 5, and 10 mg/mL, respectively. The same concentrations of components were retained in the binary systems. Rheological properties of the gels were determined using a rheometer with plane/plane geometry, and texture analysis was conducted through TPA. These findings enabled the assessment of food gel’s properties, such as hardness, springiness, chewiness, and cohesiveness. The structural characteristics of the gels were determined by SAXS, offering insights into the interactions between C-PC, BLG, and starch after HP processing. Adding C-PC and starch formed solid gels with a larger mesh than the pure BLG gels. SEM scans of the gel surface revealed that all components influenced the overall morphology of gels. Adding starch notably influenced the gels’ visual appearance and mechanical properties, even at low concentrations. Interestingly, the presence of C-PC substantially increases the gel’s solubility in water. Our investigation highlights HP treatment’s superior effectiveness in preserving C-PC compared to high temperature treatment, evidenced by the sustained colour integrity of the C-PC blue chromophore.
PB  - International Hellenic University
C3  - Food Colloids Conference, Using colloid science to find new sustainable solutions in food, Book of Abstracts, 14-18 April 2024, Thessaloniki
T1  - The use of starch and β-lactoglobulin composite hydrogels as frameworks for preserving c-phycocyanin
SP  - 267
EP  - 267
UR  - https://hdl.handle.net/21.15107/rcub_cer_7607
ER  - 

@conference{
author = "Jovanović, Zorana and Gligorijević, Nikola and Annighöfer, Burkhard and Dudzinski, Daniel and Nikolić, Milan and Pavlović, Vladimir and Lević, Steva and Brûlet, Annie and Assifaoui, Ali and Combet, Sophie and Minić, Simeon",
year = "2024",
abstract = "C-Phycocyanin (C-PC), the natural blue dye and the major protein in Spirulina, has high potential in the food industry due to its vivid colour and bioactive properties. However, low stability limits C-PC application potential, requiring approaches to strengthen its stability. Our study aimed to preserve C-PC by its incorporation into hydrogels formed by combining starch and β-lactoglobulin (BLG) using high-pressure (HP) processing. Notably, thermal treatment resulted in the complete loss of colour derived from C-PC. We performed a comprehensive characterization of the resulting HP gels by rheology measurements, texture profile analysis (TPA), small-angle X-ray scattering (SAXS), and scanning electron microscopy (SEM). Different compositions of binary (BLG/C-PC) and ternary (starch/BLG/C-PC) systems were processed under high-pressure (HP) conditions reaching up to 4,500 bar. The C-PC pigment was effectively preserved by mixing BLG and starch with C-PC at pH 7, maintaining concentrations of 180, 5, and 10 mg/mL, respectively. The same concentrations of components were retained in the binary systems. Rheological properties of the gels were determined using a rheometer with plane/plane geometry, and texture analysis was conducted through TPA. These findings enabled the assessment of food gel’s properties, such as hardness, springiness, chewiness, and cohesiveness. The structural characteristics of the gels were determined by SAXS, offering insights into the interactions between C-PC, BLG, and starch after HP processing. Adding C-PC and starch formed solid gels with a larger mesh than the pure BLG gels. SEM scans of the gel surface revealed that all components influenced the overall morphology of gels. Adding starch notably influenced the gels’ visual appearance and mechanical properties, even at low concentrations. Interestingly, the presence of C-PC substantially increases the gel’s solubility in water. Our investigation highlights HP treatment’s superior effectiveness in preserving C-PC compared to high temperature treatment, evidenced by the sustained colour integrity of the C-PC blue chromophore.",
publisher = "International Hellenic University",
journal = "Food Colloids Conference, Using colloid science to find new sustainable solutions in food, Book of Abstracts, 14-18 April 2024, Thessaloniki",
title = "The use of starch and β-lactoglobulin composite hydrogels as frameworks for preserving c-phycocyanin",
pages = "267-267",
url = "https://hdl.handle.net/21.15107/rcub_cer_7607"
}

Jovanović, Z., Gligorijević, N., Annighöfer, B., Dudzinski, D., Nikolić, M., Pavlović, V., Lević, S., Brûlet, A., Assifaoui, A., Combet, S.,& Minić, S.. (2024). The use of starch and β-lactoglobulin composite hydrogels as frameworks for preserving c-phycocyanin. in Food Colloids Conference, Using colloid science to find new sustainable solutions in food, Book of Abstracts, 14-18 April 2024, Thessaloniki
International Hellenic University., 267-267.
https://hdl.handle.net/21.15107/rcub_cer_7607

Jovanović Z, Gligorijević N, Annighöfer B, Dudzinski D, Nikolić M, Pavlović V, Lević S, Brûlet A, Assifaoui A, Combet S, Minić S. The use of starch and β-lactoglobulin composite hydrogels as frameworks for preserving c-phycocyanin. in Food Colloids Conference, Using colloid science to find new sustainable solutions in food, Book of Abstracts, 14-18 April 2024, Thessaloniki. 2024;:267-267.
https://hdl.handle.net/21.15107/rcub_cer_7607 .

Jovanović, Zorana, Gligorijević, Nikola, Annighöfer, Burkhard, Dudzinski, Daniel, Nikolić, Milan, Pavlović, Vladimir, Lević, Steva, Brûlet, Annie, Assifaoui, Ali, Combet, Sophie, Minić, Simeon, "The use of starch and β-lactoglobulin composite hydrogels as frameworks for preserving c-phycocyanin" in Food Colloids Conference, Using colloid science to find new sustainable solutions in food, Book of Abstracts, 14-18 April 2024, Thessaloniki (2024):267-267,
https://hdl.handle.net/21.15107/rcub_cer_7607 .

TY  - JOUR
AU  - Radović, Jelena
AU  - Popović, Dragana
AU  - Ćurčić, Tatjana
AU  - Veličković, Luka
AU  - Lević, Steva
AU  - Pavlović, Vladimir
AU  - Minić, Simeon
AU  - Nikolić, Milan
AU  - Gligorijević, Nikola
PY  - 2024
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/7596
AB  - Mercury emissions represent a significant risk to the environment and human health. Mercury is persistent and
can circulate in the environment for thousands of years, which is why treating this toxic metal is important.
Chitosan polymer is easily obtainable, and it has good mercury adsorption characteristics. This study aimed to
improve its capabilities to absorb mercury by immobilizing phycobiliproteins (PBPs) onto the surface of chitosan
beads (chitosan–PBPs). Phycobiliproteins, light-harvesting proteins from algae and cyanobacteria, have several
industrially essential applications. These proteins can bind heavy metals with high affinities. Protein extracts
obtained from both Arthrospira platensis, with C-phycocyanin (C-PC) as the primary protein, and Porphyra
yezoensis, with R-phycocyanin (R-PC) and R-phycoerythrin (R-PE) as the dominant PBPs, were covalently
immobilized onto chitosan beads. Beads with immobilized PBPs were characterized by scanning electron microscopy
and Fourier transform infrared spectroscopy. Binding analysis showed that, on average, each chitosan
bead weighed 20 mg and immobilized 63.54 μg of PBPs from Spirulina and 44.12 μg of PBPs from Porphyra.
Immobilized proteins were still in their native state, with no visible color change months after immobilization.
Chitosan–PBPs and chitosan alone were tested for mercury adsorption at pH 4 and pH 7 by atomic absorption
spectroscopy. The tested concentration range of mercury was from 1 to 70 ppm. Affinity, calculated using
Henry’s binding isotherm, of chitosan–PBPs for mercury was twice as much higher at both pH values than
chitosan alone. Furthermore, chitosan-PBP beads were able to absorb more mercury than chitosan alone. These
results showed that the covalent immobilization of PBPs onto chitosan improves its mercury adsorption characteristics
and creates a more efficient eco-friendly adsorbent to potentially remove mercury ions in the tested
concentration range from polluted waters.
PB  - Elsevier
T2  - Algal Research
T1  - Probing the potential of mercury removal by covalently immobilized phycobiliproteins onto the surface of chitosan beads
VL  - 80
SP  - 103543
DO  - 10.1016/j.algal.2024.103543
ER  - 

@article{
author = "Radović, Jelena and Popović, Dragana and Ćurčić, Tatjana and Veličković, Luka and Lević, Steva and Pavlović, Vladimir and Minić, Simeon and Nikolić, Milan and Gligorijević, Nikola",
year = "2024",
abstract = "Mercury emissions represent a significant risk to the environment and human health. Mercury is persistent and
can circulate in the environment for thousands of years, which is why treating this toxic metal is important.
Chitosan polymer is easily obtainable, and it has good mercury adsorption characteristics. This study aimed to
improve its capabilities to absorb mercury by immobilizing phycobiliproteins (PBPs) onto the surface of chitosan
beads (chitosan–PBPs). Phycobiliproteins, light-harvesting proteins from algae and cyanobacteria, have several
industrially essential applications. These proteins can bind heavy metals with high affinities. Protein extracts
obtained from both Arthrospira platensis, with C-phycocyanin (C-PC) as the primary protein, and Porphyra
yezoensis, with R-phycocyanin (R-PC) and R-phycoerythrin (R-PE) as the dominant PBPs, were covalently
immobilized onto chitosan beads. Beads with immobilized PBPs were characterized by scanning electron microscopy
and Fourier transform infrared spectroscopy. Binding analysis showed that, on average, each chitosan
bead weighed 20 mg and immobilized 63.54 μg of PBPs from Spirulina and 44.12 μg of PBPs from Porphyra.
Immobilized proteins were still in their native state, with no visible color change months after immobilization.
Chitosan–PBPs and chitosan alone were tested for mercury adsorption at pH 4 and pH 7 by atomic absorption
spectroscopy. The tested concentration range of mercury was from 1 to 70 ppm. Affinity, calculated using
Henry’s binding isotherm, of chitosan–PBPs for mercury was twice as much higher at both pH values than
chitosan alone. Furthermore, chitosan-PBP beads were able to absorb more mercury than chitosan alone. These
results showed that the covalent immobilization of PBPs onto chitosan improves its mercury adsorption characteristics
and creates a more efficient eco-friendly adsorbent to potentially remove mercury ions in the tested
concentration range from polluted waters.",
publisher = "Elsevier",
journal = "Algal Research",
title = "Probing the potential of mercury removal by covalently immobilized phycobiliproteins onto the surface of chitosan beads",
volume = "80",
pages = "103543",
doi = "10.1016/j.algal.2024.103543"
}

Radović, J., Popović, D., Ćurčić, T., Veličković, L., Lević, S., Pavlović, V., Minić, S., Nikolić, M.,& Gligorijević, N.. (2024). Probing the potential of mercury removal by covalently immobilized phycobiliproteins onto the surface of chitosan beads. in Algal Research
Elsevier., 80, 103543.
https://doi.org/10.1016/j.algal.2024.103543

Radović J, Popović D, Ćurčić T, Veličković L, Lević S, Pavlović V, Minić S, Nikolić M, Gligorijević N. Probing the potential of mercury removal by covalently immobilized phycobiliproteins onto the surface of chitosan beads. in Algal Research. 2024;80:103543.
doi:10.1016/j.algal.2024.103543 .

Radović, Jelena, Popović, Dragana, Ćurčić, Tatjana, Veličković, Luka, Lević, Steva, Pavlović, Vladimir, Minić, Simeon, Nikolić, Milan, Gligorijević, Nikola, "Probing the potential of mercury removal by covalently immobilized phycobiliproteins onto the surface of chitosan beads" in Algal Research, 80 (2024):103543,
https://doi.org/10.1016/j.algal.2024.103543 . .

TY  - JOUR
AU  - Minić, Simeon
AU  - Gligorijević, Nikola
AU  - Veličković, Luka
AU  - Nikolić, Milan
PY  - 2024
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/7687
AB  - Vivid-colored phycobiliproteins (PBPs) have emerging potential as food colors and alternative
proteins in the food industry. However, enhancing their application potential requires increasing
stability, cost-effective purification processes, and consumer acceptance. This narrative review aimed
to highlight information regarding the critical aspects of PBP research that is needed to improve their
food industry potential, such as stability, food fortification, development of new PBP-based food
products, and cost-effective production. The main results of the literature review show that polysaccharide
and protein-based encapsulations significantly improve PBPs’ stability. Additionally, while
many studies have investigated the ability of PBPs to enhance the techno-functional properties, like
viscosity, emulsifying and stabilizing activity, texture, rheology, etc., of widely used food products,
highly concentrated PBP food products are still rare. Therefore, much effort should be invested in
improving the stability, yield, and sensory characteristics of the PBP-fortified food due to the resulting
unpleasant sensory characteristics. Considering that most studies focus on the C-phycocyanin from
Spirulina, future studies should concentrate on less explored PBPs from red macroalgae due to their
much higher production potential, a critical factor for positioning PBPs as alternative proteins.
PB  - Multidisciplinary Digital Publishing Institute (MDPI)
T2  - International Journal of Molecular Sciences
T1  - Narrative Review of the Current and Future Perspectives of Phycobiliproteins’ Applications in the Food Industry: From Natural Colors to Alternative Proteins
VL  - 25
IS  - 13
SP  - 7187
DO  - 10.3390/ijms25137187
ER  - 

@article{
author = "Minić, Simeon and Gligorijević, Nikola and Veličković, Luka and Nikolić, Milan",
year = "2024",
abstract = "Vivid-colored phycobiliproteins (PBPs) have emerging potential as food colors and alternative
proteins in the food industry. However, enhancing their application potential requires increasing
stability, cost-effective purification processes, and consumer acceptance. This narrative review aimed
to highlight information regarding the critical aspects of PBP research that is needed to improve their
food industry potential, such as stability, food fortification, development of new PBP-based food
products, and cost-effective production. The main results of the literature review show that polysaccharide
and protein-based encapsulations significantly improve PBPs’ stability. Additionally, while
many studies have investigated the ability of PBPs to enhance the techno-functional properties, like
viscosity, emulsifying and stabilizing activity, texture, rheology, etc., of widely used food products,
highly concentrated PBP food products are still rare. Therefore, much effort should be invested in
improving the stability, yield, and sensory characteristics of the PBP-fortified food due to the resulting
unpleasant sensory characteristics. Considering that most studies focus on the C-phycocyanin from
Spirulina, future studies should concentrate on less explored PBPs from red macroalgae due to their
much higher production potential, a critical factor for positioning PBPs as alternative proteins.",
publisher = "Multidisciplinary Digital Publishing Institute (MDPI)",
journal = "International Journal of Molecular Sciences",
title = "Narrative Review of the Current and Future Perspectives of Phycobiliproteins’ Applications in the Food Industry: From Natural Colors to Alternative Proteins",
volume = "25",
number = "13",
pages = "7187",
doi = "10.3390/ijms25137187"
}

Minić, S., Gligorijević, N., Veličković, L.,& Nikolić, M.. (2024). Narrative Review of the Current and Future Perspectives of Phycobiliproteins’ Applications in the Food Industry: From Natural Colors to Alternative Proteins. in International Journal of Molecular Sciences
Multidisciplinary Digital Publishing Institute (MDPI)., 25(13), 7187.
https://doi.org/10.3390/ijms25137187

Minić S, Gligorijević N, Veličković L, Nikolić M. Narrative Review of the Current and Future Perspectives of Phycobiliproteins’ Applications in the Food Industry: From Natural Colors to Alternative Proteins. in International Journal of Molecular Sciences. 2024;25(13):7187.
doi:10.3390/ijms25137187 .

Minić, Simeon, Gligorijević, Nikola, Veličković, Luka, Nikolić, Milan, "Narrative Review of the Current and Future Perspectives of Phycobiliproteins’ Applications in the Food Industry: From Natural Colors to Alternative Proteins" in International Journal of Molecular Sciences, 25, no. 13 (2024):7187,
https://doi.org/10.3390/ijms25137187 . .

TY  - JOUR
AU  - Gligorijević, Nikola
AU  - Jovanović, Zorana
AU  - Cvijetić, Ilija
AU  - Šunderić, Miloš
AU  - Veličković, Luka
AU  - Katrlík, Jaroslav
AU  - Holazová, Alena
AU  - Nikolić, Milan
AU  - Minić, Simeon
PY  - 2024
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/7298
AB  - Blue C-phycocyanin (C-PC), the major Spirulina protein with innumerable
health-promoting benefits, is an attractive colourant and food supplement. A crucial obstacle to its
more extensive use is its relatively low stability. This study aimed to screen various food-derived
ligands for their ability to bind and stabilise C-PC, utilising spectroscopic techniques and molecular
docking. Among twelve examined ligands, the protein fluorescence quenching revealed that
only quercetin, coenzyme Q10 and resveratrol had a moderate affinity to C-PC (Ka of 2.2 to 3.7 × 105
M–1). Docking revealed these three ligands bind more strongly to the C-PC hexamer than the trimer,
with the binding sites located at the interface of two (αβ)3 trimers. UV/VIS absorption spectroscopy
demonstrated the changes in the C-PC absorption spectra in a complex with quercetin
and resveratrol compared to the spectra of free protein and ligands. Selected ligands did not affect
the secondary structure content, but they induced changes in the tertiary protein structure in the
CD study. A fluorescence-based thermal stability assay demonstrated quercetin and coenzyme Q10
increased the C-PC melting point by nearly 5 °C. Our study identified food-derived ligands that
interact with C-PC and improve its thermal stability, indicating their potential as stabilising agents
for C-PC in the food industry.
PB  - MDPI
T2  - International Journal of Molecular Sciences
T1  - Investigation of the Potential of Selected Food-Derived Antioxidants to Bind and Stabilise the Bioactive Blue Protein C-Phycocyanin from Cyanobacteria Spirulina
VL  - 25
IS  - 1
SP  - 229
DO  - 10.3390/ijms25010229
ER  - 

@article{
author = "Gligorijević, Nikola and Jovanović, Zorana and Cvijetić, Ilija and Šunderić, Miloš and Veličković, Luka and Katrlík, Jaroslav and Holazová, Alena and Nikolić, Milan and Minić, Simeon",
year = "2024",
abstract = "Blue C-phycocyanin (C-PC), the major Spirulina protein with innumerable
health-promoting benefits, is an attractive colourant and food supplement. A crucial obstacle to its
more extensive use is its relatively low stability. This study aimed to screen various food-derived
ligands for their ability to bind and stabilise C-PC, utilising spectroscopic techniques and molecular
docking. Among twelve examined ligands, the protein fluorescence quenching revealed that
only quercetin, coenzyme Q10 and resveratrol had a moderate affinity to C-PC (Ka of 2.2 to 3.7 × 105
M–1). Docking revealed these three ligands bind more strongly to the C-PC hexamer than the trimer,
with the binding sites located at the interface of two (αβ)3 trimers. UV/VIS absorption spectroscopy
demonstrated the changes in the C-PC absorption spectra in a complex with quercetin
and resveratrol compared to the spectra of free protein and ligands. Selected ligands did not affect
the secondary structure content, but they induced changes in the tertiary protein structure in the
CD study. A fluorescence-based thermal stability assay demonstrated quercetin and coenzyme Q10
increased the C-PC melting point by nearly 5 °C. Our study identified food-derived ligands that
interact with C-PC and improve its thermal stability, indicating their potential as stabilising agents
for C-PC in the food industry.",
publisher = "MDPI",
journal = "International Journal of Molecular Sciences",
title = "Investigation of the Potential of Selected Food-Derived Antioxidants to Bind and Stabilise the Bioactive Blue Protein C-Phycocyanin from Cyanobacteria Spirulina",
volume = "25",
number = "1",
pages = "229",
doi = "10.3390/ijms25010229"
}

Gligorijević, N., Jovanović, Z., Cvijetić, I., Šunderić, M., Veličković, L., Katrlík, J., Holazová, A., Nikolić, M.,& Minić, S.. (2024). Investigation of the Potential of Selected Food-Derived Antioxidants to Bind and Stabilise the Bioactive Blue Protein C-Phycocyanin from Cyanobacteria Spirulina. in International Journal of Molecular Sciences
MDPI., 25(1), 229.
https://doi.org/10.3390/ijms25010229

Gligorijević N, Jovanović Z, Cvijetić I, Šunderić M, Veličković L, Katrlík J, Holazová A, Nikolić M, Minić S. Investigation of the Potential of Selected Food-Derived Antioxidants to Bind and Stabilise the Bioactive Blue Protein C-Phycocyanin from Cyanobacteria Spirulina. in International Journal of Molecular Sciences. 2024;25(1):229.
doi:10.3390/ijms25010229 .

Gligorijević, Nikola, Jovanović, Zorana, Cvijetić, Ilija, Šunderić, Miloš, Veličković, Luka, Katrlík, Jaroslav, Holazová, Alena, Nikolić, Milan, Minić, Simeon, "Investigation of the Potential of Selected Food-Derived Antioxidants to Bind and Stabilise the Bioactive Blue Protein C-Phycocyanin from Cyanobacteria Spirulina" in International Journal of Molecular Sciences, 25, no. 1 (2024):229,
https://doi.org/10.3390/ijms25010229 . .

TY  - JOUR
AU  - Minić, Simeon
AU  - Veličković, Luka
AU  - Annighöfer, Burkhard
AU  - Thureau, Aurélien
AU  - Gligorijević, Nikola
AU  - Jovanović, Zorana
AU  - Brûlet, Annie
AU  - Combet, Sophie
PY  - 2024
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/7805
AB  - The red macroalgae Porphyra, commonly known as Nori, is widely used as food around the world due to its high nutrient content, including the significant abundance of colored phycobiliproteins (PBPs). Among these, R-phycocyanin (R-PC) stands out for its vibrant purple color and numerous bioactive properties, making it a valuable protein for the food industry. However, R-PC's limited thermal stability necessitates alternative processing methods to preserve its color and bioactive properties. Our study aimed to investigate the in-situ stability of oligomeric R-PC under high pressure (HP) conditions (up to 4000 bar) using a combination of absorption, fluorescence, and small-angle X-ray scattering (SAXS) techniques. The unfolding of R-PC is a multiphase process. Initially, low pressure induces conformational changes in the R-PC oligomeric form (trimers). As pressure increases above 1600 bar, these trimers dissociate into monomers, and at pressures above 3000 bar, the subunits begin to unfold. When returned to atmospheric pressure, R-PC partially refolds, retaining 50% of its original color absorbance. In contrast, heat treatment causes irreversible and detrimental effects on R-PC color, highlighting the advantages of HP treatment in preserving both the color and bioactive properties of R-PC compared to heat treatment.
PB  - Wiley
T2  - Protein Science
T1  - Probing the structural stability of R-phycocyanin under pressure
VL  - 33
IS  - 9
SP  - e5145
DO  - 10.1002/pro.5145
ER  - 

@article{
author = "Minić, Simeon and Veličković, Luka and Annighöfer, Burkhard and Thureau, Aurélien and Gligorijević, Nikola and Jovanović, Zorana and Brûlet, Annie and Combet, Sophie",
year = "2024",
abstract = "The red macroalgae Porphyra, commonly known as Nori, is widely used as food around the world due to its high nutrient content, including the significant abundance of colored phycobiliproteins (PBPs). Among these, R-phycocyanin (R-PC) stands out for its vibrant purple color and numerous bioactive properties, making it a valuable protein for the food industry. However, R-PC's limited thermal stability necessitates alternative processing methods to preserve its color and bioactive properties. Our study aimed to investigate the in-situ stability of oligomeric R-PC under high pressure (HP) conditions (up to 4000 bar) using a combination of absorption, fluorescence, and small-angle X-ray scattering (SAXS) techniques. The unfolding of R-PC is a multiphase process. Initially, low pressure induces conformational changes in the R-PC oligomeric form (trimers). As pressure increases above 1600 bar, these trimers dissociate into monomers, and at pressures above 3000 bar, the subunits begin to unfold. When returned to atmospheric pressure, R-PC partially refolds, retaining 50% of its original color absorbance. In contrast, heat treatment causes irreversible and detrimental effects on R-PC color, highlighting the advantages of HP treatment in preserving both the color and bioactive properties of R-PC compared to heat treatment.",
publisher = "Wiley",
journal = "Protein Science",
title = "Probing the structural stability of R-phycocyanin under pressure",
volume = "33",
number = "9",
pages = "e5145",
doi = "10.1002/pro.5145"
}

Minić, S., Veličković, L., Annighöfer, B., Thureau, A., Gligorijević, N., Jovanović, Z., Brûlet, A.,& Combet, S.. (2024). Probing the structural stability of R-phycocyanin under pressure. in Protein Science
Wiley., 33(9), e5145.
https://doi.org/10.1002/pro.5145

Minić S, Veličković L, Annighöfer B, Thureau A, Gligorijević N, Jovanović Z, Brûlet A, Combet S. Probing the structural stability of R-phycocyanin under pressure. in Protein Science. 2024;33(9):e5145.
doi:10.1002/pro.5145 .

Minić, Simeon, Veličković, Luka, Annighöfer, Burkhard, Thureau, Aurélien, Gligorijević, Nikola, Jovanović, Zorana, Brûlet, Annie, Combet, Sophie, "Probing the structural stability of R-phycocyanin under pressure" in Protein Science, 33, no. 9 (2024):e5145,
https://doi.org/10.1002/pro.5145 . .

TY  - JOUR
AU  - Radomirović, Mirjana
AU  - Gligorijević, Nikola
AU  - Stanić-Vučinić, Dragana
AU  - Nikolić, Milan
AU  - Ćirković-Veličković, Tanja
PY  - 2024
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/7645
AB  - BACKGROUND: Phycocyanobilin (PCB) is an open-chain blue tetrapyrrole chromophore of C-phycocyanin (C-PC), a major chromoprotein
derived from the cyanobacterium Arthrospira platensis having numerous health-promoting effects. Relying on the
ability of PCB to attach to the sulfhydryl group of proteins, we propose a new method for covalent attachment of PCB to bovine
serum albumin (BSA) as a means of its functionalization.
RESULTS: Traut's reagent (TR, 2-iminothiolane), modifying lysine residues, was used to optimize the introduction of sulfhydryl
groups in BSA. A higher degree of BSA thiolation by TR induces more profound alterations of its structure, resulting in minor
oligomerization and aggregation. A 50-fold molar excess of TR was found to be the optimal, balancing thiolation level and
adverse effect on protein structure. PCB was covalently attached to newly introduced sulfhydryl groups at pH 9 at 20-fold
PCB/BSA ratio. An increase in the TR/BSA molar ratio leads to increased efficiency of PCB conjugation with thiolated BSA. Compared
to native BSA, BSA–PCB conjugate binds quercetin with similar affinity but has higher antioxidant activity and increased
oxidative stability.
CONCLUSIONS: PCB-modified BSA could serve as a stable, food-compatible carrier of bioactive PCB, but also bind other ligands
that would be protected from oxidative damage due to the high antioxidant potential of covalently bound PCB. Thiolation by
TR is, at the same time, a simple method for the covalent functionalization of virtually any protein by bioactive PCB or for
obtaining PCB-based fluorescent probes.
PB  - Wiley
T2  - Journal of the Science of Food and Agriculture
T1  - Fabrication and characterization of bovine serum albumin–phycocyanobilin conjugate: effect on antioxidant and ligand-binding properties
DO  - 10.1002/jsfa.13649
ER  - 

@article{
author = "Radomirović, Mirjana and Gligorijević, Nikola and Stanić-Vučinić, Dragana and Nikolić, Milan and Ćirković-Veličković, Tanja",
year = "2024",
abstract = "BACKGROUND: Phycocyanobilin (PCB) is an open-chain blue tetrapyrrole chromophore of C-phycocyanin (C-PC), a major chromoprotein
derived from the cyanobacterium Arthrospira platensis having numerous health-promoting effects. Relying on the
ability of PCB to attach to the sulfhydryl group of proteins, we propose a new method for covalent attachment of PCB to bovine
serum albumin (BSA) as a means of its functionalization.
RESULTS: Traut's reagent (TR, 2-iminothiolane), modifying lysine residues, was used to optimize the introduction of sulfhydryl
groups in BSA. A higher degree of BSA thiolation by TR induces more profound alterations of its structure, resulting in minor
oligomerization and aggregation. A 50-fold molar excess of TR was found to be the optimal, balancing thiolation level and
adverse effect on protein structure. PCB was covalently attached to newly introduced sulfhydryl groups at pH 9 at 20-fold
PCB/BSA ratio. An increase in the TR/BSA molar ratio leads to increased efficiency of PCB conjugation with thiolated BSA. Compared
to native BSA, BSA–PCB conjugate binds quercetin with similar affinity but has higher antioxidant activity and increased
oxidative stability.
CONCLUSIONS: PCB-modified BSA could serve as a stable, food-compatible carrier of bioactive PCB, but also bind other ligands
that would be protected from oxidative damage due to the high antioxidant potential of covalently bound PCB. Thiolation by
TR is, at the same time, a simple method for the covalent functionalization of virtually any protein by bioactive PCB or for
obtaining PCB-based fluorescent probes.",
publisher = "Wiley",
journal = "Journal of the Science of Food and Agriculture",
title = "Fabrication and characterization of bovine serum albumin–phycocyanobilin conjugate: effect on antioxidant and ligand-binding properties",
doi = "10.1002/jsfa.13649"
}

Radomirović, M., Gligorijević, N., Stanić-Vučinić, D., Nikolić, M.,& Ćirković-Veličković, T.. (2024). Fabrication and characterization of bovine serum albumin–phycocyanobilin conjugate: effect on antioxidant and ligand-binding properties. in Journal of the Science of Food and Agriculture
Wiley..
https://doi.org/10.1002/jsfa.13649

Radomirović M, Gligorijević N, Stanić-Vučinić D, Nikolić M, Ćirković-Veličković T. Fabrication and characterization of bovine serum albumin–phycocyanobilin conjugate: effect on antioxidant and ligand-binding properties. in Journal of the Science of Food and Agriculture. 2024;.
doi:10.1002/jsfa.13649 .

Radomirović, Mirjana, Gligorijević, Nikola, Stanić-Vučinić, Dragana, Nikolić, Milan, Ćirković-Veličković, Tanja, "Fabrication and characterization of bovine serum albumin–phycocyanobilin conjugate: effect on antioxidant and ligand-binding properties" in Journal of the Science of Food and Agriculture (2024),
https://doi.org/10.1002/jsfa.13649 . .

TY  - CONF
AU  - Obradović, Milan
AU  - Zafirović, Sonja
AU  - Šundrić, Miloš
AU  - Gligorijević, Nikola
AU  - Banjac, Katarina
AU  - Nedić, Olgica
AU  - Isenović, Esma
PY  - 2024
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/7766
UR  - https://www.rad-conference.org/RAD_2024-Book_of_Abstracts.pdf
AB  - Insulin-like growth factor binding (IGFB) proteins are a group of six highly conserved proteins that bind to insulin-like growth factors (IGFs) and transport them through the bloodstream to the target cells. The IGFB proteins play an important role in regulating IGF signaling pathways by lengthening their half-life. Obesity and associated disorders are linked to abnormal levels of IGFB proteins. Thus, this study aimed to evaluate how IGF-1 affects the levels of IGFB proteins in the serum of obese rats.
PB  - Niš, Serbia : RAD Centre
C3  - Twelfth International Conference on Radiation, Natural Sciences, Medicine, Engineering, Technology and Ecology (RAD 2024 Conference), Book of Abstracts, June 17-21, 2024, Herceg Novi, Montenegro
T1  - Effects of IGF-1 on the IGFB proteins level in the serum of obese male rats
SP  - 8
EP  - 8
UR  - https://hdl.handle.net/21.15107/rcub_cer_7766
ER  - 

@conference{
author = "Obradović, Milan and Zafirović, Sonja and Šundrić, Miloš and Gligorijević, Nikola and Banjac, Katarina and Nedić, Olgica and Isenović, Esma",
year = "2024",
abstract = "Insulin-like growth factor binding (IGFB) proteins are a group of six highly conserved proteins that bind to insulin-like growth factors (IGFs) and transport them through the bloodstream to the target cells. The IGFB proteins play an important role in regulating IGF signaling pathways by lengthening their half-life. Obesity and associated disorders are linked to abnormal levels of IGFB proteins. Thus, this study aimed to evaluate how IGF-1 affects the levels of IGFB proteins in the serum of obese rats.",
publisher = "Niš, Serbia : RAD Centre",
journal = "Twelfth International Conference on Radiation, Natural Sciences, Medicine, Engineering, Technology and Ecology (RAD 2024 Conference), Book of Abstracts, June 17-21, 2024, Herceg Novi, Montenegro",
title = "Effects of IGF-1 on the IGFB proteins level in the serum of obese male rats",
pages = "8-8",
url = "https://hdl.handle.net/21.15107/rcub_cer_7766"
}

Obradović, M., Zafirović, S., Šundrić, M., Gligorijević, N., Banjac, K., Nedić, O.,& Isenović, E.. (2024). Effects of IGF-1 on the IGFB proteins level in the serum of obese male rats. in Twelfth International Conference on Radiation, Natural Sciences, Medicine, Engineering, Technology and Ecology (RAD 2024 Conference), Book of Abstracts, June 17-21, 2024, Herceg Novi, Montenegro
Niš, Serbia : RAD Centre., 8-8.
https://hdl.handle.net/21.15107/rcub_cer_7766

Obradović M, Zafirović S, Šundrić M, Gligorijević N, Banjac K, Nedić O, Isenović E. Effects of IGF-1 on the IGFB proteins level in the serum of obese male rats. in Twelfth International Conference on Radiation, Natural Sciences, Medicine, Engineering, Technology and Ecology (RAD 2024 Conference), Book of Abstracts, June 17-21, 2024, Herceg Novi, Montenegro. 2024;:8-8.
https://hdl.handle.net/21.15107/rcub_cer_7766 .

Obradović, Milan, Zafirović, Sonja, Šundrić, Miloš, Gligorijević, Nikola, Banjac, Katarina, Nedić, Olgica, Isenović, Esma, "Effects of IGF-1 on the IGFB proteins level in the serum of obese male rats" in Twelfth International Conference on Radiation, Natural Sciences, Medicine, Engineering, Technology and Ecology (RAD 2024 Conference), Book of Abstracts, June 17-21, 2024, Herceg Novi, Montenegro (2024):8-8,
https://hdl.handle.net/21.15107/rcub_cer_7766 .

TY  - CONF
AU  - Tubić, Lora
AU  - Dragić, Milorad
AU  - Nikolić, Marija S.
AU  - Nikolić, Milan
AU  - Gligorijević, Nikola
AU  - Minić, Simeon
PY  - 2024
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/7690
AB  - Hydrogels play a significant role in the food industry as three-dimensional polymer networks.
Hydrogels have found extensive use not only in the production of traditional food products but also
in designing carriers for bioactive components. Developing hydrogels for food applications
prioritizes the use of natural ingredients and simple production methods. Extracts from the red
microalgae Porphyridium purpureum contain sulphated polysaccharides and vibrantly coloured
phycobiliproteins (PBPs), notably B-Phycoerythrin. This makes Porphyridium purpureum an
excellent starting point for developing food-based hydrogels with strong bioactive properties. This
work aims to develop and characterize the hydrogels from water extracts of Porphyridium
purpureum. In order to achieve that, we used the gelling property of the extract under acidic
conditions at pH 2.0. Two types of hydrogels based on this algal extract were compared. The first is
formed solely in an acidic environment, while the second is formed by adding alginate at the same
pH in the presence of calcium ions. The mechanical properties of both hydrogels were determined
by frequency sweep measurements using a rheometer with applied plane/plane geometry.
Rheological measurements showed that adding alginate significantly increases the mechanical
properties and elasticity of the hydrogel. Confocal microscopy demonstrated stronger fluorescence
of PBPs in the gel without alginate. Furthermore, the distribution of different PBPs within the gel
network is more uniform without alginate. The digestibility of the hydrogels was evaluated using an
in vitro static digestion model. Although both hydrogels were confirmed to be digestible, the
hydrogel without adding alginate showed higher digestibility. Antioxidant assays, ABTS and a
reducing power test showed that bioaccessible peptides after digestion of both hydrogels possess
antioxidant activity, with those obtained without alginate having a higher activity. Overall, this
research provides a simple and effective approach for developing coloured hydrogels with attractive
appearance, good bioaccessibility and notable bioactive properties.
PB  - Faculty of Agriculture
C3  - UNIFood2024 Conference, 3rd International UNIfood Conference, Book of Abstracts, June 28-29, 2024, Belgrade, Serbia
T1  - Composite hydrogels obtained from extracts of Porphyridium purpureum and alginate
SP  - 164
EP  - 164
UR  - https://hdl.handle.net/21.15107/rcub_cer_7690
ER  - 

@conference{
author = "Tubić, Lora and Dragić, Milorad and Nikolić, Marija S. and Nikolić, Milan and Gligorijević, Nikola and Minić, Simeon",
year = "2024",
abstract = "Hydrogels play a significant role in the food industry as three-dimensional polymer networks.
Hydrogels have found extensive use not only in the production of traditional food products but also
in designing carriers for bioactive components. Developing hydrogels for food applications
prioritizes the use of natural ingredients and simple production methods. Extracts from the red
microalgae Porphyridium purpureum contain sulphated polysaccharides and vibrantly coloured
phycobiliproteins (PBPs), notably B-Phycoerythrin. This makes Porphyridium purpureum an
excellent starting point for developing food-based hydrogels with strong bioactive properties. This
work aims to develop and characterize the hydrogels from water extracts of Porphyridium
purpureum. In order to achieve that, we used the gelling property of the extract under acidic
conditions at pH 2.0. Two types of hydrogels based on this algal extract were compared. The first is
formed solely in an acidic environment, while the second is formed by adding alginate at the same
pH in the presence of calcium ions. The mechanical properties of both hydrogels were determined
by frequency sweep measurements using a rheometer with applied plane/plane geometry.
Rheological measurements showed that adding alginate significantly increases the mechanical
properties and elasticity of the hydrogel. Confocal microscopy demonstrated stronger fluorescence
of PBPs in the gel without alginate. Furthermore, the distribution of different PBPs within the gel
network is more uniform without alginate. The digestibility of the hydrogels was evaluated using an
in vitro static digestion model. Although both hydrogels were confirmed to be digestible, the
hydrogel without adding alginate showed higher digestibility. Antioxidant assays, ABTS and a
reducing power test showed that bioaccessible peptides after digestion of both hydrogels possess
antioxidant activity, with those obtained without alginate having a higher activity. Overall, this
research provides a simple and effective approach for developing coloured hydrogels with attractive
appearance, good bioaccessibility and notable bioactive properties.",
publisher = "Faculty of Agriculture",
journal = "UNIFood2024 Conference, 3rd International UNIfood Conference, Book of Abstracts, June 28-29, 2024, Belgrade, Serbia",
title = "Composite hydrogels obtained from extracts of Porphyridium purpureum and alginate",
pages = "164-164",
url = "https://hdl.handle.net/21.15107/rcub_cer_7690"
}

Tubić, L., Dragić, M., Nikolić, M. S., Nikolić, M., Gligorijević, N.,& Minić, S.. (2024). Composite hydrogels obtained from extracts of Porphyridium purpureum and alginate. in UNIFood2024 Conference, 3rd International UNIfood Conference, Book of Abstracts, June 28-29, 2024, Belgrade, Serbia
Faculty of Agriculture., 164-164.
https://hdl.handle.net/21.15107/rcub_cer_7690

Tubić L, Dragić M, Nikolić MS, Nikolić M, Gligorijević N, Minić S. Composite hydrogels obtained from extracts of Porphyridium purpureum and alginate. in UNIFood2024 Conference, 3rd International UNIfood Conference, Book of Abstracts, June 28-29, 2024, Belgrade, Serbia. 2024;:164-164.
https://hdl.handle.net/21.15107/rcub_cer_7690 .

Tubić, Lora, Dragić, Milorad, Nikolić, Marija S., Nikolić, Milan, Gligorijević, Nikola, Minić, Simeon, "Composite hydrogels obtained from extracts of Porphyridium purpureum and alginate" in UNIFood2024 Conference, 3rd International UNIfood Conference, Book of Abstracts, June 28-29, 2024, Belgrade, Serbia (2024):164-164,
https://hdl.handle.net/21.15107/rcub_cer_7690 .

TY  - CONF
AU  - Lujić, Tamara
AU  - Krstić-Ristivojević, Maja
AU  - Gligorijević, Nikola
AU  - Stanić-Vučinić, Dragana
AU  - Wimmer, Lukas
AU  - Dailey, Lea Ann
AU  - Ćirković-Veličković, Tanja
PY  - 2024
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/7686
AB  - Trypsin is the main protease in the intestine. Microplastics (MPs) have been previously shown to interact with and decrease the activity of some digestive enzymes, including pepsin and lipase. Red meat has been shown to be a source of allergy which has been linked to the galactose-alpha-1,3-galactose (alpha-Gal) post-translational modification of proteins. Our aim was to investigate the effect of two types of MPs commonly found in the environment – polypropylene (PP) and polyethylene terephthalate (PET) – on the digestion of protein in beef meat extract and preservation of protein harboring the alpha-Gal epitope. Digestion of beef meat extract has been performed with trypsin in simulated intestinal fluid (SIF) in the presence of MPs. After digestion was stopped with a specific inhibitor, bulk beef meat extract was separated through centrifugation from the MPs. Soft coronas were obtained by washing the MPs with SIF. The hard corona was obtained by addition of a reducing buffer for electrophoresis sample preparation to the MPs with a heating step at 95°C. All samples were analyzed with SDS-PAG electrophoresis. Selected samples were further analyzed with anti-alpha-Gal antibodies using western blot. There is an observable difference between the digestion patterns of meat extract after 1 and 2 h of digestion in the presence of MPs compared to the control. Evolution of digestion is similar for both types of MPs, without regard to plastic type. It has also been confirmed that preserved proteins possess the alpha-Gal modification. As MPs presence does not change trypsin specific activity, the change in digestion pattern is presumed to be due to steric effects and/or interplay of enzyme/protein in the corona. This study suggests that MPs presence influences trypsin digestibility of meat proteins, including alpha-Gal-bearing allergens.
PB  - FEBS Press
C3  - FEBS openbio, 48th FEBS Congress, 29 June - 3 July 2024, Milano Italy
T1  - Trypsin digestion of protein in beef meat extract in the presence of microplastics
VL  - 14
IS  - Supplement 2
SP  - 428
EP  - 428
DO  - 10.1002/2211-5463.13837
ER  - 

@conference{
author = "Lujić, Tamara and Krstić-Ristivojević, Maja and Gligorijević, Nikola and Stanić-Vučinić, Dragana and Wimmer, Lukas and Dailey, Lea Ann and Ćirković-Veličković, Tanja",
year = "2024",
abstract = "Trypsin is the main protease in the intestine. Microplastics (MPs) have been previously shown to interact with and decrease the activity of some digestive enzymes, including pepsin and lipase. Red meat has been shown to be a source of allergy which has been linked to the galactose-alpha-1,3-galactose (alpha-Gal) post-translational modification of proteins. Our aim was to investigate the effect of two types of MPs commonly found in the environment – polypropylene (PP) and polyethylene terephthalate (PET) – on the digestion of protein in beef meat extract and preservation of protein harboring the alpha-Gal epitope. Digestion of beef meat extract has been performed with trypsin in simulated intestinal fluid (SIF) in the presence of MPs. After digestion was stopped with a specific inhibitor, bulk beef meat extract was separated through centrifugation from the MPs. Soft coronas were obtained by washing the MPs with SIF. The hard corona was obtained by addition of a reducing buffer for electrophoresis sample preparation to the MPs with a heating step at 95°C. All samples were analyzed with SDS-PAG electrophoresis. Selected samples were further analyzed with anti-alpha-Gal antibodies using western blot. There is an observable difference between the digestion patterns of meat extract after 1 and 2 h of digestion in the presence of MPs compared to the control. Evolution of digestion is similar for both types of MPs, without regard to plastic type. It has also been confirmed that preserved proteins possess the alpha-Gal modification. As MPs presence does not change trypsin specific activity, the change in digestion pattern is presumed to be due to steric effects and/or interplay of enzyme/protein in the corona. This study suggests that MPs presence influences trypsin digestibility of meat proteins, including alpha-Gal-bearing allergens.",
publisher = "FEBS Press",
journal = "FEBS openbio, 48th FEBS Congress, 29 June - 3 July 2024, Milano Italy",
title = "Trypsin digestion of protein in beef meat extract in the presence of microplastics",
volume = "14",
number = "Supplement 2",
pages = "428-428",
doi = "10.1002/2211-5463.13837"
}

Lujić, T., Krstić-Ristivojević, M., Gligorijević, N., Stanić-Vučinić, D., Wimmer, L., Dailey, L. A.,& Ćirković-Veličković, T.. (2024). Trypsin digestion of protein in beef meat extract in the presence of microplastics. in FEBS openbio, 48th FEBS Congress, 29 June - 3 July 2024, Milano Italy
FEBS Press., 14(Supplement 2), 428-428.
https://doi.org/10.1002/2211-5463.13837

Lujić T, Krstić-Ristivojević M, Gligorijević N, Stanić-Vučinić D, Wimmer L, Dailey LA, Ćirković-Veličković T. Trypsin digestion of protein in beef meat extract in the presence of microplastics. in FEBS openbio, 48th FEBS Congress, 29 June - 3 July 2024, Milano Italy. 2024;14(Supplement 2):428-428.
doi:10.1002/2211-5463.13837 .

Lujić, Tamara, Krstić-Ristivojević, Maja, Gligorijević, Nikola, Stanić-Vučinić, Dragana, Wimmer, Lukas, Dailey, Lea Ann, Ćirković-Veličković, Tanja, "Trypsin digestion of protein in beef meat extract in the presence of microplastics" in FEBS openbio, 48th FEBS Congress, 29 June - 3 July 2024, Milano Italy, 14, no. Supplement 2 (2024):428-428,
https://doi.org/10.1002/2211-5463.13837 . .

TY  - JOUR
AU  - Gligorijević, Nikola
AU  - Lujić, Tamara
AU  - Mutić, Tamara
AU  - Vasović, Tamara
AU  - de Guzman, Maria Krishna
AU  - Aćimović, Jelena
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2024
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/7606
AB  - Contaminating microplastics can interact with food proteins in the food matrix and during digestion. This study investigated adsorption of chicken egg protein ovalbumin to polystyrene (PS, 110 and 260 μm) and polyethylene terephthalate (PET, 140 μm) MPs in acidic and neutral conditions and alterations in ovalbumin structure. Ovalbumin adsorption affinity depended on MPs size (smaller > larger), type (PS > PET) and pH (pH 3 > pH 7). In bulk solution, MPs does not change ovalbumin secondary structure significantly, but induces loosening (at pH 3) and tightening (at pH 7) of tertiary structure. Formed soft corona exclusively consists of full length non-native ovalbumin, while in hard corona also shorter ovalbumin fragments were found. At pH 7 soft corona ovalbumin has rearranged but still preserved level of ordered secondary structure, resulting in preserved thermostability and proteolytic stability, but decreased ability to form fibrils upon heating. Secondary structure changes in soft corona resemble changes in native ovalbumin induced by heat treatment (80 ◦C). Ovalbumin is abundantly present in corona around microplastics also in the presence of other egg white proteins. These results imply that microplastics contaminating food may bind and change structure and functional properties of the main egg white protein.
PB  - Elsevier
T2  - International Journal of Biological Macromolecules
T1  - Ovalbumin interaction with polystyrene and polyethylene terephthalate microplastics alters its structural properties
VL  - 267
SP  - 131564
DO  - 10.1016/j.ijbiomac.2024.131564
ER  - 

@article{
author = "Gligorijević, Nikola and Lujić, Tamara and Mutić, Tamara and Vasović, Tamara and de Guzman, Maria Krishna and Aćimović, Jelena and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2024",
abstract = "Contaminating microplastics can interact with food proteins in the food matrix and during digestion. This study investigated adsorption of chicken egg protein ovalbumin to polystyrene (PS, 110 and 260 μm) and polyethylene terephthalate (PET, 140 μm) MPs in acidic and neutral conditions and alterations in ovalbumin structure. Ovalbumin adsorption affinity depended on MPs size (smaller > larger), type (PS > PET) and pH (pH 3 > pH 7). In bulk solution, MPs does not change ovalbumin secondary structure significantly, but induces loosening (at pH 3) and tightening (at pH 7) of tertiary structure. Formed soft corona exclusively consists of full length non-native ovalbumin, while in hard corona also shorter ovalbumin fragments were found. At pH 7 soft corona ovalbumin has rearranged but still preserved level of ordered secondary structure, resulting in preserved thermostability and proteolytic stability, but decreased ability to form fibrils upon heating. Secondary structure changes in soft corona resemble changes in native ovalbumin induced by heat treatment (80 ◦C). Ovalbumin is abundantly present in corona around microplastics also in the presence of other egg white proteins. These results imply that microplastics contaminating food may bind and change structure and functional properties of the main egg white protein.",
publisher = "Elsevier",
journal = "International Journal of Biological Macromolecules",
title = "Ovalbumin interaction with polystyrene and polyethylene terephthalate microplastics alters its structural properties",
volume = "267",
pages = "131564",
doi = "10.1016/j.ijbiomac.2024.131564"
}

Gligorijević, N., Lujić, T., Mutić, T., Vasović, T., de Guzman, M. K., Aćimović, J., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2024). Ovalbumin interaction with polystyrene and polyethylene terephthalate microplastics alters its structural properties. in International Journal of Biological Macromolecules
Elsevier., 267, 131564.
https://doi.org/10.1016/j.ijbiomac.2024.131564

Gligorijević N, Lujić T, Mutić T, Vasović T, de Guzman MK, Aćimović J, Stanić-Vučinić D, Ćirković-Veličković T. Ovalbumin interaction with polystyrene and polyethylene terephthalate microplastics alters its structural properties. in International Journal of Biological Macromolecules. 2024;267:131564.
doi:10.1016/j.ijbiomac.2024.131564 .

Gligorijević, Nikola, Lujić, Tamara, Mutić, Tamara, Vasović, Tamara, de Guzman, Maria Krishna, Aćimović, Jelena, Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Ovalbumin interaction with polystyrene and polyethylene terephthalate microplastics alters its structural properties" in International Journal of Biological Macromolecules, 267 (2024):131564,
https://doi.org/10.1016/j.ijbiomac.2024.131564 . .

TY  - CONF
AU  - Aćimović, Jelena
AU  - Gligorijević, Nikola
AU  - Radomirović, Mirjana
AU  - Vasović, Tamara
AU  - Stojadinović, Marija
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2024
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/7649
AB  - Microplastics (MPs) interact with proteins, forming a complex called a protein corona. This corona
alters the biological identity and properties of MPs, enabling them to evade the immune system,
persist longer in circulation, and disrupt cellular and molecular processes. Biofilm formation on
MPs occurs in several steps, starting with initial binding of molecules to form a hard corona,
followed by the formation of a soft corona. β-Lactoglobulin (BLG), a major whey protein in bovine
milk, is highly valued as a food ingredient but poses significant health risks to milk-allergic
individuals. This study aimed to understand BLG's interactions with selected MPs (polyethylene
terephthalate, PET, <80μm; polypropylene, PP, 63-180μm). BLG, isolated from
unpasteurized/pasteurized milk, was incubated with PP and PET in simulated physiological fluids.
The resulting coronas were analyzed using reduced SDS-PAGE electrophoresis and densitometry.
BLG exhibited low binding to both MPs, with pasteurized BLG showing the lowest binding to PP
(less than 1% of control in its soft corona). There were differences in the protein content of hard
coronas between pasteurized and unpasteurized BLG, with a slightly higher percentage of bound
proteins in the hard corona of unpasteurized BLG. Additionally, the protein profile of hard coronas
differed between PET and PP incubated with pasteurized BLG compared to those with
unpasteurized BLG. These findings suggest that the presence of MPs may affect the bioavailability
and allergenic properties of both pasteurized and unpasteurized BLG.
AB  - Interakcija mikroplastike (MP) s proteinima stvara kompleks poznat kao proteinska korona. U okviru korone, MP dobija nove biološke osobine, uključujući izbegavanje imunog sistema, dugotrajnije zadržavanje u cirkulaciji i ometanje ćelijskih procesa. Formiranje biofilma na površini MP je višestepeni proces, gde se nakon prvobitnog vezivanja molekula s visokim afinitetom i formiranja čvrste korone, može razviti i labavija korona u kasnijim fazama. β-laktoglobulin (BLG), glavni protein u surutki kravljeg mleka, često korišćen u hrani, može izazvati značajne zdravstvene probleme kod osoba alergičnih na mleko. Ovo istraživanje je imalo za cilj da pruži bolji uvid u interakcije između BLG kao alergena hrane i odabranih MP (polietilen-tereftalat, PET, <80μm; polipropilen, PP, 63-180μm). Izolovani nepasterizovani/pasterizovani BLG je inkubiran s PP i PET in vitro, u simuliranim fiziološkim tečnostima, a formirane korone su analizirane SDSPAGE elektroforezom pod redukujućim uslovima i denzitometrijom. Rezultati pokazuju da BLG slabo vezuje za obe MP. Postoji razlika u proteinima čvrstih korona između pasterizovanog i nepasterizovanog BLG, kao i u proteinskom profilu korona PP i PET inkubiranih s pasterizovanim ili nepasterizovanim BLG. Naši rezultati ukazuju da prisustvo MP može uticati na biodostupnost i alergene osobine i pasterizovanog i nepasterizovanog BLG.
PB  - Serbian Chemical Society
PB  - Srpsko hemijsko društvo
C3  - 60. Savetovanje Srpskog hemijskog društva - Kratki izvodi radova, Niš 8. i 9. jun 2024. godine
T1  - Soft i hard korona mikroplastike u interakciji sa alergenom β-laktoglobulinom kravljeg mleka
T1  - Soft and hard corona of microplastics interacted with allergenic bovine milk β-lactoglobulin
SP  - 53
EP  - 53
UR  - https://hdl.handle.net/21.15107/rcub_cer_7649
ER  - 

@conference{
author = "Aćimović, Jelena and Gligorijević, Nikola and Radomirović, Mirjana and Vasović, Tamara and Stojadinović, Marija and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2024",
abstract = "Microplastics (MPs) interact with proteins, forming a complex called a protein corona. This corona
alters the biological identity and properties of MPs, enabling them to evade the immune system,
persist longer in circulation, and disrupt cellular and molecular processes. Biofilm formation on
MPs occurs in several steps, starting with initial binding of molecules to form a hard corona,
followed by the formation of a soft corona. β-Lactoglobulin (BLG), a major whey protein in bovine
milk, is highly valued as a food ingredient but poses significant health risks to milk-allergic
individuals. This study aimed to understand BLG's interactions with selected MPs (polyethylene
terephthalate, PET, <80μm; polypropylene, PP, 63-180μm). BLG, isolated from
unpasteurized/pasteurized milk, was incubated with PP and PET in simulated physiological fluids.
The resulting coronas were analyzed using reduced SDS-PAGE electrophoresis and densitometry.
BLG exhibited low binding to both MPs, with pasteurized BLG showing the lowest binding to PP
(less than 1% of control in its soft corona). There were differences in the protein content of hard
coronas between pasteurized and unpasteurized BLG, with a slightly higher percentage of bound
proteins in the hard corona of unpasteurized BLG. Additionally, the protein profile of hard coronas
differed between PET and PP incubated with pasteurized BLG compared to those with
unpasteurized BLG. These findings suggest that the presence of MPs may affect the bioavailability
and allergenic properties of both pasteurized and unpasteurized BLG., Interakcija mikroplastike (MP) s proteinima stvara kompleks poznat kao proteinska korona. U okviru korone, MP dobija nove biološke osobine, uključujući izbegavanje imunog sistema, dugotrajnije zadržavanje u cirkulaciji i ometanje ćelijskih procesa. Formiranje biofilma na površini MP je višestepeni proces, gde se nakon prvobitnog vezivanja molekula s visokim afinitetom i formiranja čvrste korone, može razviti i labavija korona u kasnijim fazama. β-laktoglobulin (BLG), glavni protein u surutki kravljeg mleka, često korišćen u hrani, može izazvati značajne zdravstvene probleme kod osoba alergičnih na mleko. Ovo istraživanje je imalo za cilj da pruži bolji uvid u interakcije između BLG kao alergena hrane i odabranih MP (polietilen-tereftalat, PET, <80μm; polipropilen, PP, 63-180μm). Izolovani nepasterizovani/pasterizovani BLG je inkubiran s PP i PET in vitro, u simuliranim fiziološkim tečnostima, a formirane korone su analizirane SDSPAGE elektroforezom pod redukujućim uslovima i denzitometrijom. Rezultati pokazuju da BLG slabo vezuje za obe MP. Postoji razlika u proteinima čvrstih korona između pasterizovanog i nepasterizovanog BLG, kao i u proteinskom profilu korona PP i PET inkubiranih s pasterizovanim ili nepasterizovanim BLG. Naši rezultati ukazuju da prisustvo MP može uticati na biodostupnost i alergene osobine i pasterizovanog i nepasterizovanog BLG.",
publisher = "Serbian Chemical Society, Srpsko hemijsko društvo",
journal = "60. Savetovanje Srpskog hemijskog društva - Kratki izvodi radova, Niš 8. i 9. jun 2024. godine",
title = "Soft i hard korona mikroplastike u interakciji sa alergenom β-laktoglobulinom kravljeg mleka, Soft and hard corona of microplastics interacted with allergenic bovine milk β-lactoglobulin",
pages = "53-53",
url = "https://hdl.handle.net/21.15107/rcub_cer_7649"
}

Aćimović, J., Gligorijević, N., Radomirović, M., Vasović, T., Stojadinović, M., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2024). Soft i hard korona mikroplastike u interakciji sa alergenom β-laktoglobulinom kravljeg mleka. in 60. Savetovanje Srpskog hemijskog društva - Kratki izvodi radova, Niš 8. i 9. jun 2024. godine
Serbian Chemical Society., 53-53.
https://hdl.handle.net/21.15107/rcub_cer_7649

Aćimović J, Gligorijević N, Radomirović M, Vasović T, Stojadinović M, Stanić-Vučinić D, Ćirković-Veličković T. Soft i hard korona mikroplastike u interakciji sa alergenom β-laktoglobulinom kravljeg mleka. in 60. Savetovanje Srpskog hemijskog društva - Kratki izvodi radova, Niš 8. i 9. jun 2024. godine. 2024;:53-53.
https://hdl.handle.net/21.15107/rcub_cer_7649 .

Aćimović, Jelena, Gligorijević, Nikola, Radomirović, Mirjana, Vasović, Tamara, Stojadinović, Marija, Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Soft i hard korona mikroplastike u interakciji sa alergenom β-laktoglobulinom kravljeg mleka" in 60. Savetovanje Srpskog hemijskog društva - Kratki izvodi radova, Niš 8. i 9. jun 2024. godine (2024):53-53,
https://hdl.handle.net/21.15107/rcub_cer_7649 .

TY  - JOUR
AU  - Miljuš, Goran
AU  - Penezić, Ana
AU  - Pažitná, Lucia
AU  - Gligorijević, Nikola
AU  - Baralić, Marko
AU  - Vilotić, Aleksandra
AU  - Šunderić, Miloš
AU  - Robajac, Dragana
AU  - Dobrijević, Zorana
AU  - Katrlík, Jaroslav
AU  - Nedić, Olgica
PY  - 2024
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/7597
AB  - Chronic kidney disease (CKD) is a global health concern affecting approximately one billion individuals worldwide. End-stage kidney disease (ESKD), the most severe form of CKD, is
often accompanied by anemia. Peritoneal dialysis (PD), a common treatment for ESKD, utilizes the
peritoneum for solute transfer but is associated with complications including protein loss, including
transferrin (Tf) a key protein involved in iron transport. This study investigated Tf characteristics in
ESKD patients compared to healthy individuals using lectin microarray, spectroscopic techniques and immunocytochemical analysis to assess Tf interaction with transferrin receptors (TfRs). ESKD patients exhibited altered Tf glycosylation patterns, evidenced by significant changes in lectin reactivity compared to healthy controls. However, structural analyses revealed no significant differences in the Tf secondary or tertiary structures between the two groups. A functional analysis demonstrated comparable Tf-TfR interaction in both PD and healthy samples. Despite significant alterations in Tf glycosylation, structural integrity and Tf-TfR interaction remained preserved in PD patients. These findings suggest that while glycosylation changes may influence iron metabolism, they do not impair Tf function. The study highlights the importance of a glucose-free dialysis solutions in managing anemia exacerbation in PD patients with poorly controlled anemia, potentially offering a targeted therapeutic approach to improve patient outcomes.
PB  - Multidisciplinary Digital Publishing Institute (MDPI)
T2  - International Journal of Molecular Sciences
T1  - Glycosylation and Characterization of Human Transferrin in an End-Stage Kidney Disease
VL  - 25
IS  - 9
SP  - 4625
DO  - 10.3390/ijms25094625
ER  - 

@article{
author = "Miljuš, Goran and Penezić, Ana and Pažitná, Lucia and Gligorijević, Nikola and Baralić, Marko and Vilotić, Aleksandra and Šunderić, Miloš and Robajac, Dragana and Dobrijević, Zorana and Katrlík, Jaroslav and Nedić, Olgica",
year = "2024",
abstract = "Chronic kidney disease (CKD) is a global health concern affecting approximately one billion individuals worldwide. End-stage kidney disease (ESKD), the most severe form of CKD, is
often accompanied by anemia. Peritoneal dialysis (PD), a common treatment for ESKD, utilizes the
peritoneum for solute transfer but is associated with complications including protein loss, including
transferrin (Tf) a key protein involved in iron transport. This study investigated Tf characteristics in
ESKD patients compared to healthy individuals using lectin microarray, spectroscopic techniques and immunocytochemical analysis to assess Tf interaction with transferrin receptors (TfRs). ESKD patients exhibited altered Tf glycosylation patterns, evidenced by significant changes in lectin reactivity compared to healthy controls. However, structural analyses revealed no significant differences in the Tf secondary or tertiary structures between the two groups. A functional analysis demonstrated comparable Tf-TfR interaction in both PD and healthy samples. Despite significant alterations in Tf glycosylation, structural integrity and Tf-TfR interaction remained preserved in PD patients. These findings suggest that while glycosylation changes may influence iron metabolism, they do not impair Tf function. The study highlights the importance of a glucose-free dialysis solutions in managing anemia exacerbation in PD patients with poorly controlled anemia, potentially offering a targeted therapeutic approach to improve patient outcomes.",
publisher = "Multidisciplinary Digital Publishing Institute (MDPI)",
journal = "International Journal of Molecular Sciences",
title = "Glycosylation and Characterization of Human Transferrin in an End-Stage Kidney Disease",
volume = "25",
number = "9",
pages = "4625",
doi = "10.3390/ijms25094625"
}

Miljuš, G., Penezić, A., Pažitná, L., Gligorijević, N., Baralić, M., Vilotić, A., Šunderić, M., Robajac, D., Dobrijević, Z., Katrlík, J.,& Nedić, O.. (2024). Glycosylation and Characterization of Human Transferrin in an End-Stage Kidney Disease. in International Journal of Molecular Sciences
Multidisciplinary Digital Publishing Institute (MDPI)., 25(9), 4625.
https://doi.org/10.3390/ijms25094625

Miljuš G, Penezić A, Pažitná L, Gligorijević N, Baralić M, Vilotić A, Šunderić M, Robajac D, Dobrijević Z, Katrlík J, Nedić O. Glycosylation and Characterization of Human Transferrin in an End-Stage Kidney Disease. in International Journal of Molecular Sciences. 2024;25(9):4625.
doi:10.3390/ijms25094625 .

Miljuš, Goran, Penezić, Ana, Pažitná, Lucia, Gligorijević, Nikola, Baralić, Marko, Vilotić, Aleksandra, Šunderić, Miloš, Robajac, Dragana, Dobrijević, Zorana, Katrlík, Jaroslav, Nedić, Olgica, "Glycosylation and Characterization of Human Transferrin in an End-Stage Kidney Disease" in International Journal of Molecular Sciences, 25, no. 9 (2024):4625,
https://doi.org/10.3390/ijms25094625 . .

TY  - CONF
AU  - Jovanović, Zorana
AU  - Annighöfer, Burkhard
AU  - Dudzinski, Daniel
AU  - Gligorijević, Nikola
AU  - Nikolić, Milan
AU  - Pavlović, Vladimir B.
AU  - Lević, Steva
AU  - Brûlet, Annie
AU  - Assifaoui, Ali
AU  - Combet, Sophie
AU  - Minić, Simeon
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/7521
AB  - Our study aimed to preserve the natural blue dye of C-phycocyanin (C-PC)
phycobiliprotein from Spirulina microalgae due to its importance in the food industry. We
incorporated C-PC into hydrogels formed by combining starch and β-lactoglobulin (BLG)
using high-pressure (HP) processing to achieve this objective. Notably, thermal treatment
resulted in the complete loss of colour derived from C-PC.
We performed a comprehensive characterization of the resulting HP gels by rheology
measurements, texture profile analysis (TPA), small-angle X-ray scattering (SAXS), and
scanning electron microscopy (SEM).
Different compositions of binary (BLG/C-PC) and ternary (starch/BLG/C-PC)
systems were processed under high-pressure (HP) conditions reaching up to 4,500 bar. The
C-PC pigment was effectively preserved by mixing BLG and starch with C-PC at pH 7,
maintaining concentrations of 180, 5, and 10 mg/mL, respectively. The same concentrations
of components were retained in the binary systems.
Rheological properties of the gels were determined using a rheometer with
plane/plane geometry, and texture analysis was conducted through TPA. These findings
enabled the assessment of food gel's properties, such as hardness, springiness, chewiness, and
cohesiveness. The structural characteristics of the gels were determined by SAXS, offering
insights into the interactions between C-PC, BLG, and starch after HP processing. Adding CPC
and starch formed solid gels with a larger mesh than the pure BLG gels. SEM scans of the
gel surface revealed that all components influenced the overall morphology of gels. Even at
low concentrations, the addition of starch notably influenced the gels' visual appearance and
mechanical properties. Our investigation highlights the superior effectiveness of HP treatment
in the preservation of C-PC compared to high-temperature treatment, evident in the sustained
colour integrity of the C-PC blue dye.
PB  - Faculty of Technology and Metallurgy, University of Belgrade
C3  - Book of abstracts - International Conference on Biochemical Engineering and Biotechnology for Young Scientists, Belgrade
T1  - The use of starch and β-lactoglobulin composite hydrogels as frameworks for preserving c-phycocyanin
SP  - 60
EP  - 60
UR  - https://hdl.handle.net/21.15107/rcub_cer_7521
ER  - 

@conference{
author = "Jovanović, Zorana and Annighöfer, Burkhard and Dudzinski, Daniel and Gligorijević, Nikola and Nikolić, Milan and Pavlović, Vladimir B. and Lević, Steva and Brûlet, Annie and Assifaoui, Ali and Combet, Sophie and Minić, Simeon",
year = "2023",
abstract = "Our study aimed to preserve the natural blue dye of C-phycocyanin (C-PC)
phycobiliprotein from Spirulina microalgae due to its importance in the food industry. We
incorporated C-PC into hydrogels formed by combining starch and β-lactoglobulin (BLG)
using high-pressure (HP) processing to achieve this objective. Notably, thermal treatment
resulted in the complete loss of colour derived from C-PC.
We performed a comprehensive characterization of the resulting HP gels by rheology
measurements, texture profile analysis (TPA), small-angle X-ray scattering (SAXS), and
scanning electron microscopy (SEM).
Different compositions of binary (BLG/C-PC) and ternary (starch/BLG/C-PC)
systems were processed under high-pressure (HP) conditions reaching up to 4,500 bar. The
C-PC pigment was effectively preserved by mixing BLG and starch with C-PC at pH 7,
maintaining concentrations of 180, 5, and 10 mg/mL, respectively. The same concentrations
of components were retained in the binary systems.
Rheological properties of the gels were determined using a rheometer with
plane/plane geometry, and texture analysis was conducted through TPA. These findings
enabled the assessment of food gel's properties, such as hardness, springiness, chewiness, and
cohesiveness. The structural characteristics of the gels were determined by SAXS, offering
insights into the interactions between C-PC, BLG, and starch after HP processing. Adding CPC
and starch formed solid gels with a larger mesh than the pure BLG gels. SEM scans of the
gel surface revealed that all components influenced the overall morphology of gels. Even at
low concentrations, the addition of starch notably influenced the gels' visual appearance and
mechanical properties. Our investigation highlights the superior effectiveness of HP treatment
in the preservation of C-PC compared to high-temperature treatment, evident in the sustained
colour integrity of the C-PC blue dye.",
publisher = "Faculty of Technology and Metallurgy, University of Belgrade",
journal = "Book of abstracts - International Conference on Biochemical Engineering and Biotechnology for Young Scientists, Belgrade",
title = "The use of starch and β-lactoglobulin composite hydrogels as frameworks for preserving c-phycocyanin",
pages = "60-60",
url = "https://hdl.handle.net/21.15107/rcub_cer_7521"
}

Jovanović, Z., Annighöfer, B., Dudzinski, D., Gligorijević, N., Nikolić, M., Pavlović, V. B., Lević, S., Brûlet, A., Assifaoui, A., Combet, S.,& Minić, S.. (2023). The use of starch and β-lactoglobulin composite hydrogels as frameworks for preserving c-phycocyanin. in Book of abstracts - International Conference on Biochemical Engineering and Biotechnology for Young Scientists, Belgrade
Faculty of Technology and Metallurgy, University of Belgrade., 60-60.
https://hdl.handle.net/21.15107/rcub_cer_7521

Jovanović Z, Annighöfer B, Dudzinski D, Gligorijević N, Nikolić M, Pavlović VB, Lević S, Brûlet A, Assifaoui A, Combet S, Minić S. The use of starch and β-lactoglobulin composite hydrogels as frameworks for preserving c-phycocyanin. in Book of abstracts - International Conference on Biochemical Engineering and Biotechnology for Young Scientists, Belgrade. 2023;:60-60.
https://hdl.handle.net/21.15107/rcub_cer_7521 .

Jovanović, Zorana, Annighöfer, Burkhard, Dudzinski, Daniel, Gligorijević, Nikola, Nikolić, Milan, Pavlović, Vladimir B., Lević, Steva, Brûlet, Annie, Assifaoui, Ali, Combet, Sophie, Minić, Simeon, "The use of starch and β-lactoglobulin composite hydrogels as frameworks for preserving c-phycocyanin" in Book of abstracts - International Conference on Biochemical Engineering and Biotechnology for Young Scientists, Belgrade (2023):60-60,
https://hdl.handle.net/21.15107/rcub_cer_7521 .

TY  - JOUR
AU  - Radomirović, Mirjana
AU  - Gligorijević, Nikola
AU  - Stanić-Vučinić, Dragana
AU  - Rajković, Andreja
AU  - Ćirković Veličković, Tanja
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6782
AB  - Tropomyosin is the major and predominant allergen among shellfish. This study developed
an ultrasensitive immuno-PCR method for the quantification of crustacean tropomyosin in foods.
The method couples sandwich ELISA with the real-time PCR (rtPCR) amplification of marker DNAs.
Monoclonal anti-TPM antibody was the capture antibody, polyclonal rabbit anti-shrimp tropomyosin
antibody was the detection antibody, while natural shrimp tropomyosin served as the standard. A
double-stranded amino-DNA was covalently conjugated to a secondary anti-rabbit antibody and
subsequently amplified and quantified via rtPCR. The quantification sensitivity of immuno-PCR
was 20-fold higher than analogous ELISA, with LOQ 19.8 pg/mL. The developed immuno-PCR
method is highly specific for the detection of crustacean tropomyosin and is highly precise in a
broad concentration range. Tropomyosin recovery in the spiked vegetable soup was 87.7–115.6%.
Crustacean tropomyosin was also quantified in commercial food products. The reported immuno-
PCR assay is the most sensitive method for the quantification of crustacean tropomyosin and is the
first immuno-PCR-based assay for the quantification of food allergen and food protein in general.
The described method could be easily adapted for the specific and ultrasensitive immuno-PCR-based
detection of traces of any food allergen that is currently being quantified with ELISA, which is of
critical importance for people with food allergies.
PB  - MDPI
T2  - International Journal of Molecular Sciences
T1  - Ultrasensitive Quantification of Crustacean Tropomyosin by Immuno-PCR
VL  - 24
IS  - 20
SP  - 15410
DO  - 10.3390/ijms242015410
ER  - 

@article{
author = "Radomirović, Mirjana and Gligorijević, Nikola and Stanić-Vučinić, Dragana and Rajković, Andreja and Ćirković Veličković, Tanja",
year = "2023",
abstract = "Tropomyosin is the major and predominant allergen among shellfish. This study developed
an ultrasensitive immuno-PCR method for the quantification of crustacean tropomyosin in foods.
The method couples sandwich ELISA with the real-time PCR (rtPCR) amplification of marker DNAs.
Monoclonal anti-TPM antibody was the capture antibody, polyclonal rabbit anti-shrimp tropomyosin
antibody was the detection antibody, while natural shrimp tropomyosin served as the standard. A
double-stranded amino-DNA was covalently conjugated to a secondary anti-rabbit antibody and
subsequently amplified and quantified via rtPCR. The quantification sensitivity of immuno-PCR
was 20-fold higher than analogous ELISA, with LOQ 19.8 pg/mL. The developed immuno-PCR
method is highly specific for the detection of crustacean tropomyosin and is highly precise in a
broad concentration range. Tropomyosin recovery in the spiked vegetable soup was 87.7–115.6%.
Crustacean tropomyosin was also quantified in commercial food products. The reported immuno-
PCR assay is the most sensitive method for the quantification of crustacean tropomyosin and is the
first immuno-PCR-based assay for the quantification of food allergen and food protein in general.
The described method could be easily adapted for the specific and ultrasensitive immuno-PCR-based
detection of traces of any food allergen that is currently being quantified with ELISA, which is of
critical importance for people with food allergies.",
publisher = "MDPI",
journal = "International Journal of Molecular Sciences",
title = "Ultrasensitive Quantification of Crustacean Tropomyosin by Immuno-PCR",
volume = "24",
number = "20",
pages = "15410",
doi = "10.3390/ijms242015410"
}

Radomirović, M., Gligorijević, N., Stanić-Vučinić, D., Rajković, A.,& Ćirković Veličković, T.. (2023). Ultrasensitive Quantification of Crustacean Tropomyosin by Immuno-PCR. in International Journal of Molecular Sciences
MDPI., 24(20), 15410.
https://doi.org/10.3390/ijms242015410

Radomirović M, Gligorijević N, Stanić-Vučinić D, Rajković A, Ćirković Veličković T. Ultrasensitive Quantification of Crustacean Tropomyosin by Immuno-PCR. in International Journal of Molecular Sciences. 2023;24(20):15410.
doi:10.3390/ijms242015410 .

Radomirović, Mirjana, Gligorijević, Nikola, Stanić-Vučinić, Dragana, Rajković, Andreja, Ćirković Veličković, Tanja, "Ultrasensitive Quantification of Crustacean Tropomyosin by Immuno-PCR" in International Journal of Molecular Sciences, 24, no. 20 (2023):15410,
https://doi.org/10.3390/ijms242015410 . .

TY  - JOUR
AU  - Nedić, Olgica
AU  - Penezić, Ana
AU  - Minić, Simeon
AU  - Radomirović, Mirjana
AU  - Nikolić, Milan
AU  - Ćirković Veličković, Tanja
AU  - Gligorijević, Nikola
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6485
AB  - Common to all biological systems and living organisms are molecular interactions, which
may lead to specific physiological events. Most often, a cascade of events occurs, establishing an
equilibrium between possibly competing and/or synergistic processes. Biochemical pathways that
sustain life depend on multiple intrinsic and extrinsic factors contributing to aging and/or diseases.
This article deals with food antioxidants and human proteins from the circulation, their interaction,
their effect on the structure, properties, and function of antioxidant-bound proteins, and the possible
impact of complex formation on antioxidants. An overview of studies examining interactions between
individual antioxidant compounds and major blood proteins is presented with findings. Investigating
antioxidant/protein interactions at the level of the human organism and determining antioxidant
distribution between proteins and involvement in the particular physiological role is a very complex
and challenging task. However, by knowing the role of a particular protein in certain pathology or
aging, and the effect exerted by a particular antioxidant bound to it, it is possible to recommend
specific food intake or resistance to it to improve the condition or slow down the process.
PB  - Multidisciplinary Digital Publishing Institute (MDPI)
T2  - Antioxidants
T1  - Food Antioxidants and Their Interaction with Human Proteins
VL  - 12
IS  - 4
SP  - 815
DO  - 10.3390/antiox12040815
ER  - 

@article{
author = "Nedić, Olgica and Penezić, Ana and Minić, Simeon and Radomirović, Mirjana and Nikolić, Milan and Ćirković Veličković, Tanja and Gligorijević, Nikola",
year = "2023",
abstract = "Common to all biological systems and living organisms are molecular interactions, which
may lead to specific physiological events. Most often, a cascade of events occurs, establishing an
equilibrium between possibly competing and/or synergistic processes. Biochemical pathways that
sustain life depend on multiple intrinsic and extrinsic factors contributing to aging and/or diseases.
This article deals with food antioxidants and human proteins from the circulation, their interaction,
their effect on the structure, properties, and function of antioxidant-bound proteins, and the possible
impact of complex formation on antioxidants. An overview of studies examining interactions between
individual antioxidant compounds and major blood proteins is presented with findings. Investigating
antioxidant/protein interactions at the level of the human organism and determining antioxidant
distribution between proteins and involvement in the particular physiological role is a very complex
and challenging task. However, by knowing the role of a particular protein in certain pathology or
aging, and the effect exerted by a particular antioxidant bound to it, it is possible to recommend
specific food intake or resistance to it to improve the condition or slow down the process.",
publisher = "Multidisciplinary Digital Publishing Institute (MDPI)",
journal = "Antioxidants",
title = "Food Antioxidants and Their Interaction with Human Proteins",
volume = "12",
number = "4",
pages = "815",
doi = "10.3390/antiox12040815"
}

Nedić, O., Penezić, A., Minić, S., Radomirović, M., Nikolić, M., Ćirković Veličković, T.,& Gligorijević, N.. (2023). Food Antioxidants and Their Interaction with Human Proteins. in Antioxidants
Multidisciplinary Digital Publishing Institute (MDPI)., 12(4), 815.
https://doi.org/10.3390/antiox12040815

Nedić O, Penezić A, Minić S, Radomirović M, Nikolić M, Ćirković Veličković T, Gligorijević N. Food Antioxidants and Their Interaction with Human Proteins. in Antioxidants. 2023;12(4):815.
doi:10.3390/antiox12040815 .

Nedić, Olgica, Penezić, Ana, Minić, Simeon, Radomirović, Mirjana, Nikolić, Milan, Ćirković Veličković, Tanja, Gligorijević, Nikola, "Food Antioxidants and Their Interaction with Human Proteins" in Antioxidants, 12, no. 4 (2023):815,
https://doi.org/10.3390/antiox12040815 . .

TY  - JOUR
AU  - Platanić Arizanović, Lena
AU  - Gligorijević, Nikola
AU  - Cvijetić, Ilija
AU  - Mijatović, Aleksandar
AU  - Krstić Ristivojević, Maja
AU  - Minić, Simeon
AU  - Nikolić Kokić, Aleksandra
AU  - Miljević, Čedo
AU  - Nikolić, Milan
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6482
AB  - Packed with hemoglobin, an essential protein for oxygen transport, human erythrocytes
are a suitable model system for testing the pleiotropic effects of lipophilic drugs. Our study investigated the interaction between antipsychotic drugs clozapine, ziprasidone, sertindole, and human hemoglobin under simulated physiological conditions. Analysis of protein fluorescence quenching at different temperatures and data obtained from the van’t Hoff diagram and molecular docking indicate that the interactions are static and that the tetrameric human hemoglobin has one binding site for all drugs in the central cavity near αβ  interfaces and is dominantly mediated through hydrophobic forces. The association constants were lower-moderate strength (~10^4 M^-1), the highest observed for clozapine (2.2 x 10^4 M^-1 at 25 °C). The clozapine binding showed “friendly” effects: increased α-helical content, a higher melting point, and protein protection from free radical-mediated oxidation. On the other hand, bound ziprasidone and sertindole had a slightly pro-oxidative effect, increasing ferrihemoglobin content, a possible “foe”. Since the interaction of proteins with drugs plays a vital role in their pharmacokinetic and pharmacodynamic properties, the physiological significance of the obtained findings is briefly discussed.
PB  - Multidisciplinary Digital Publishing Institute (MDPI)
T2  - International Journal of Molecular Sciences
T1  - Human Hemoglobin and Antipsychotics Clozapine, Ziprasidone and Sertindole: Friends or Foes?
VL  - 24
IS  - 10
SP  - 8921
DO  - 10.3390/ijms24108921
ER  - 

@article{
author = "Platanić Arizanović, Lena and Gligorijević, Nikola and Cvijetić, Ilija and Mijatović, Aleksandar and Krstić Ristivojević, Maja and Minić, Simeon and Nikolić Kokić, Aleksandra and Miljević, Čedo and Nikolić, Milan",
year = "2023",
abstract = "Packed with hemoglobin, an essential protein for oxygen transport, human erythrocytes
are a suitable model system for testing the pleiotropic effects of lipophilic drugs. Our study investigated the interaction between antipsychotic drugs clozapine, ziprasidone, sertindole, and human hemoglobin under simulated physiological conditions. Analysis of protein fluorescence quenching at different temperatures and data obtained from the van’t Hoff diagram and molecular docking indicate that the interactions are static and that the tetrameric human hemoglobin has one binding site for all drugs in the central cavity near αβ  interfaces and is dominantly mediated through hydrophobic forces. The association constants were lower-moderate strength (~10^4 M^-1), the highest observed for clozapine (2.2 x 10^4 M^-1 at 25 °C). The clozapine binding showed “friendly” effects: increased α-helical content, a higher melting point, and protein protection from free radical-mediated oxidation. On the other hand, bound ziprasidone and sertindole had a slightly pro-oxidative effect, increasing ferrihemoglobin content, a possible “foe”. Since the interaction of proteins with drugs plays a vital role in their pharmacokinetic and pharmacodynamic properties, the physiological significance of the obtained findings is briefly discussed.",
publisher = "Multidisciplinary Digital Publishing Institute (MDPI)",
journal = "International Journal of Molecular Sciences",
title = "Human Hemoglobin and Antipsychotics Clozapine, Ziprasidone and Sertindole: Friends or Foes?",
volume = "24",
number = "10",
pages = "8921",
doi = "10.3390/ijms24108921"
}

Platanić Arizanović, L., Gligorijević, N., Cvijetić, I., Mijatović, A., Krstić Ristivojević, M., Minić, S., Nikolić Kokić, A., Miljević, Č.,& Nikolić, M.. (2023). Human Hemoglobin and Antipsychotics Clozapine, Ziprasidone and Sertindole: Friends or Foes?. in International Journal of Molecular Sciences
Multidisciplinary Digital Publishing Institute (MDPI)., 24(10), 8921.
https://doi.org/10.3390/ijms24108921

Platanić Arizanović L, Gligorijević N, Cvijetić I, Mijatović A, Krstić Ristivojević M, Minić S, Nikolić Kokić A, Miljević Č, Nikolić M. Human Hemoglobin and Antipsychotics Clozapine, Ziprasidone and Sertindole: Friends or Foes?. in International Journal of Molecular Sciences. 2023;24(10):8921.
doi:10.3390/ijms24108921 .

Platanić Arizanović, Lena, Gligorijević, Nikola, Cvijetić, Ilija, Mijatović, Aleksandar, Krstić Ristivojević, Maja, Minić, Simeon, Nikolić Kokić, Aleksandra, Miljević, Čedo, Nikolić, Milan, "Human Hemoglobin and Antipsychotics Clozapine, Ziprasidone and Sertindole: Friends or Foes?" in International Journal of Molecular Sciences, 24, no. 10 (2023):8921,
https://doi.org/10.3390/ijms24108921 . .

TY  - JOUR
AU  - Baralić, Marko
AU  - Robajac, Dragana
AU  - Penezić, Ana
AU  - Brković, Voin
AU  - Gligorijević, Nikola
AU  - Bontić, Ana
AU  - Pavlović, Jelena
AU  - Nikolić, Jelena
AU  - Miljuš, Goran
AU  - Dobrijević, Zorana
AU  - Šunderić, Miloš
AU  - Pažitna, Lucija
AU  - Katrlík, Jaroslav
AU  - Nedić, Olgica
AU  - Laušević, Mirjana
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6445
AB  - In previous publications, we pointed out the importance of mannosylation of fibrinogen for the development of cardiovascular complications and fucosylation as a predictor of peritoneal membrane dysfunction in patients on peritoneal dialysis (PD). After a follow-up period of 30 months from the onset of the COVID-19 pandemic, we evaluated the significance of 1,25-dihydroxyvitamin D3 (calcitriol) therapy, primary disease, biochemical and hematologic analyzes, and previously performed glycan analysis by lectin-based microarray as predictors of mortality in this patient group. After univariate Cox regression analysis, diabetes mellitus (DM) and calcitriol therapy were found to be potential predictors of mortality. Additional multivariate Cox regression analysis confirmed that only DM was a predictor of mortality. Nevertheless, the use of calcitriol in therapy significantly reduced mortality in this patient group, as shown by the Kaplan–Meier survival curve. The presence of DM as a concomitant disease proved to be a strong predictor of fatal outcome in PD patients infected with SARS-CoV-2. This is the first study to indicate the importance and beneficial effect of calcitriol therapy on survival in PD patients with COVID-19 infection. In addition, this study points to the possibility that adverse thrombogenic events observed in PD patients during the pandemic may be caused by aberrant fibrinogen glycosylation.
PB  - Switzerland : Multidisciplinary Digital Publishing Institute (MDPI)
T2  - Nutrients
T1  - Significance of 1,25-Dihydroxyvitamin D3 on Overall Mortality in Peritoneal Dialysis Patients with COVID-19
VL  - 15
IS  - 9
SP  - 2050
DO  - 10.3390/nu15092050
ER  - 

@article{
author = "Baralić, Marko and Robajac, Dragana and Penezić, Ana and Brković, Voin and Gligorijević, Nikola and Bontić, Ana and Pavlović, Jelena and Nikolić, Jelena and Miljuš, Goran and Dobrijević, Zorana and Šunderić, Miloš and Pažitna, Lucija and Katrlík, Jaroslav and Nedić, Olgica and Laušević, Mirjana",
year = "2023",
abstract = "In previous publications, we pointed out the importance of mannosylation of fibrinogen for the development of cardiovascular complications and fucosylation as a predictor of peritoneal membrane dysfunction in patients on peritoneal dialysis (PD). After a follow-up period of 30 months from the onset of the COVID-19 pandemic, we evaluated the significance of 1,25-dihydroxyvitamin D3 (calcitriol) therapy, primary disease, biochemical and hematologic analyzes, and previously performed glycan analysis by lectin-based microarray as predictors of mortality in this patient group. After univariate Cox regression analysis, diabetes mellitus (DM) and calcitriol therapy were found to be potential predictors of mortality. Additional multivariate Cox regression analysis confirmed that only DM was a predictor of mortality. Nevertheless, the use of calcitriol in therapy significantly reduced mortality in this patient group, as shown by the Kaplan–Meier survival curve. The presence of DM as a concomitant disease proved to be a strong predictor of fatal outcome in PD patients infected with SARS-CoV-2. This is the first study to indicate the importance and beneficial effect of calcitriol therapy on survival in PD patients with COVID-19 infection. In addition, this study points to the possibility that adverse thrombogenic events observed in PD patients during the pandemic may be caused by aberrant fibrinogen glycosylation.",
publisher = "Switzerland : Multidisciplinary Digital Publishing Institute (MDPI)",
journal = "Nutrients",
title = "Significance of 1,25-Dihydroxyvitamin D3 on Overall Mortality in Peritoneal Dialysis Patients with COVID-19",
volume = "15",
number = "9",
pages = "2050",
doi = "10.3390/nu15092050"
}

Baralić, M., Robajac, D., Penezić, A., Brković, V., Gligorijević, N., Bontić, A., Pavlović, J., Nikolić, J., Miljuš, G., Dobrijević, Z., Šunderić, M., Pažitna, L., Katrlík, J., Nedić, O.,& Laušević, M.. (2023). Significance of 1,25-Dihydroxyvitamin D3 on Overall Mortality in Peritoneal Dialysis Patients with COVID-19. in Nutrients
Switzerland : Multidisciplinary Digital Publishing Institute (MDPI)., 15(9), 2050.
https://doi.org/10.3390/nu15092050

Baralić M, Robajac D, Penezić A, Brković V, Gligorijević N, Bontić A, Pavlović J, Nikolić J, Miljuš G, Dobrijević Z, Šunderić M, Pažitna L, Katrlík J, Nedić O, Laušević M. Significance of 1,25-Dihydroxyvitamin D3 on Overall Mortality in Peritoneal Dialysis Patients with COVID-19. in Nutrients. 2023;15(9):2050.
doi:10.3390/nu15092050 .

Baralić, Marko, Robajac, Dragana, Penezić, Ana, Brković, Voin, Gligorijević, Nikola, Bontić, Ana, Pavlović, Jelena, Nikolić, Jelena, Miljuš, Goran, Dobrijević, Zorana, Šunderić, Miloš, Pažitna, Lucija, Katrlík, Jaroslav, Nedić, Olgica, Laušević, Mirjana, "Significance of 1,25-Dihydroxyvitamin D3 on Overall Mortality in Peritoneal Dialysis Patients with COVID-19" in Nutrients, 15, no. 9 (2023):2050,
https://doi.org/10.3390/nu15092050 . .

TY  - JOUR
AU  - Šunderić, Miloš
AU  - Gligorijević, Nikola
AU  - Milčić, Miloš
AU  - Minić, Simeon
AU  - Nedić, Olgica
AU  - Nikolić, Milan
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6471
AB  - Under simulated physiological conditions, this study investigates the interaction between nutraceutical phycocyanobilin (PCB) and the universal anti-protease protein human alpha-2-macroglobulin (a2M). Extensive molecular docking analyses on multiple a2M conformations, spectroscopic techniques, and a2M activity assays were utilized to examine the complex formation. The results revealed that for every protein conformation, two high energy binding sites exist: the first, conformationally independent, at the interface region between two monomer chains and the second, conformationally dependent, in the pocket composed of amino acids from four distinct domains (TED, RBD, CUB, and MG2) of the single protein chain. Spectrofluorimetric measurements indicated a moderate affinity between a2M and PCB with a moderately high binding constant of 6.3 x 10^5 M^-1 at 25 °C. The binding of PCB to a2M resulted in minor changes in the secondary structure content of a2M. Furthermore, PCB protected a2M from oxidation and preserved its anti-protease activity in the oxidative environment. These findings suggest that PCB binding could indirectly impact the body’s response to oxidative stress by influencing a2M’s role in controlling enzyme activity during the inflammatory process.
PB  - Taylor & Francis Group
T2  - Journal of Biomolecular Structure and Dynamics
T1  - Phycocyanobilin is a new binding partner of human alpha-2-macroglobulin that protects the protein against oxidative stress
DO  - 10.1080/07391102.2023.2248273
ER  - 

@article{
author = "Šunderić, Miloš and Gligorijević, Nikola and Milčić, Miloš and Minić, Simeon and Nedić, Olgica and Nikolić, Milan",
year = "2023",
abstract = "Under simulated physiological conditions, this study investigates the interaction between nutraceutical phycocyanobilin (PCB) and the universal anti-protease protein human alpha-2-macroglobulin (a2M). Extensive molecular docking analyses on multiple a2M conformations, spectroscopic techniques, and a2M activity assays were utilized to examine the complex formation. The results revealed that for every protein conformation, two high energy binding sites exist: the first, conformationally independent, at the interface region between two monomer chains and the second, conformationally dependent, in the pocket composed of amino acids from four distinct domains (TED, RBD, CUB, and MG2) of the single protein chain. Spectrofluorimetric measurements indicated a moderate affinity between a2M and PCB with a moderately high binding constant of 6.3 x 10^5 M^-1 at 25 °C. The binding of PCB to a2M resulted in minor changes in the secondary structure content of a2M. Furthermore, PCB protected a2M from oxidation and preserved its anti-protease activity in the oxidative environment. These findings suggest that PCB binding could indirectly impact the body’s response to oxidative stress by influencing a2M’s role in controlling enzyme activity during the inflammatory process.",
publisher = "Taylor & Francis Group",
journal = "Journal of Biomolecular Structure and Dynamics",
title = "Phycocyanobilin is a new binding partner of human alpha-2-macroglobulin that protects the protein against oxidative stress",
doi = "10.1080/07391102.2023.2248273"
}

Šunderić, M., Gligorijević, N., Milčić, M., Minić, S., Nedić, O.,& Nikolić, M.. (2023). Phycocyanobilin is a new binding partner of human alpha-2-macroglobulin that protects the protein against oxidative stress. in Journal of Biomolecular Structure and Dynamics
Taylor & Francis Group..
https://doi.org/10.1080/07391102.2023.2248273

Šunderić M, Gligorijević N, Milčić M, Minić S, Nedić O, Nikolić M. Phycocyanobilin is a new binding partner of human alpha-2-macroglobulin that protects the protein against oxidative stress. in Journal of Biomolecular Structure and Dynamics. 2023;.
doi:10.1080/07391102.2023.2248273 .

Šunderić, Miloš, Gligorijević, Nikola, Milčić, Miloš, Minić, Simeon, Nedić, Olgica, Nikolić, Milan, "Phycocyanobilin is a new binding partner of human alpha-2-macroglobulin that protects the protein against oxidative stress" in Journal of Biomolecular Structure and Dynamics (2023),
https://doi.org/10.1080/07391102.2023.2248273 . .

TY  - JOUR
AU  - Veličković, Luka
AU  - Simović, Ana
AU  - Gligorijević, Nikola
AU  - Thureau, Aurelien
AU  - Obradović, Milica
AU  - Vasović, Tamara
AU  - Sotiroudis, Georgios
AU  - Zoumpanioti, Maria
AU  - Brulet, Annie
AU  - Ćirković Veličković, Tanja
AU  - Combet, Sophie
AU  - Nikolić, Milan
AU  - Minić, Simeon
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6473
AB  - This study aimed to purify, characterise and stabilise the natural food colourant, R-phycocyanin (R-PC), from the red algae Porphyra spp. (Nori). We purified R-PC from dried Nori flakes with a high purity ratio (A618/A280 ≥ 3.4) in native form (α-helix content 53%). SAXS measurements revealed that R-PC is trimeric ((αβ)3) in solution. The thermal denaturation of α-helix revealed one transition (Tm at 52 ◦C), while the pH stability study showed R-PC is stable in the pH range 4–8. The thermal treatment of R-PC at 60 °C has detrimental and irreversible effects on RPC colour and antioxidant capacity (22 % of residual capacity). However, immobilisation of R-PC within calcium alginate beads completely preserves R-PC colour and mainly retains its antioxidant ability (78 % of residual
capacity). Results give new insights into the stability of R-PC and preservation of its purple colour and bioactivity by encapsulation in calcium alginate beads.
PB  - Elsevier Ltd.
T2  - Food Chemistry
T1  - Exploring and strengthening the potential of R-phycocyanin from Nori flakes as a food colourant
VL  - 426
SP  - 136669
DO  - 10.1016/j.foodchem.2023.136669
ER  - 

@article{
author = "Veličković, Luka and Simović, Ana and Gligorijević, Nikola and Thureau, Aurelien and Obradović, Milica and Vasović, Tamara and Sotiroudis, Georgios and Zoumpanioti, Maria and Brulet, Annie and Ćirković Veličković, Tanja and Combet, Sophie and Nikolić, Milan and Minić, Simeon",
year = "2023",
abstract = "This study aimed to purify, characterise and stabilise the natural food colourant, R-phycocyanin (R-PC), from the red algae Porphyra spp. (Nori). We purified R-PC from dried Nori flakes with a high purity ratio (A618/A280 ≥ 3.4) in native form (α-helix content 53%). SAXS measurements revealed that R-PC is trimeric ((αβ)3) in solution. The thermal denaturation of α-helix revealed one transition (Tm at 52 ◦C), while the pH stability study showed R-PC is stable in the pH range 4–8. The thermal treatment of R-PC at 60 °C has detrimental and irreversible effects on RPC colour and antioxidant capacity (22 % of residual capacity). However, immobilisation of R-PC within calcium alginate beads completely preserves R-PC colour and mainly retains its antioxidant ability (78 % of residual
capacity). Results give new insights into the stability of R-PC and preservation of its purple colour and bioactivity by encapsulation in calcium alginate beads.",
publisher = "Elsevier Ltd.",
journal = "Food Chemistry",
title = "Exploring and strengthening the potential of R-phycocyanin from Nori flakes as a food colourant",
volume = "426",
pages = "136669",
doi = "10.1016/j.foodchem.2023.136669"
}

Veličković, L., Simović, A., Gligorijević, N., Thureau, A., Obradović, M., Vasović, T., Sotiroudis, G., Zoumpanioti, M., Brulet, A., Ćirković Veličković, T., Combet, S., Nikolić, M.,& Minić, S.. (2023). Exploring and strengthening the potential of R-phycocyanin from Nori flakes as a food colourant. in Food Chemistry
Elsevier Ltd.., 426, 136669.
https://doi.org/10.1016/j.foodchem.2023.136669

Veličković L, Simović A, Gligorijević N, Thureau A, Obradović M, Vasović T, Sotiroudis G, Zoumpanioti M, Brulet A, Ćirković Veličković T, Combet S, Nikolić M, Minić S. Exploring and strengthening the potential of R-phycocyanin from Nori flakes as a food colourant. in Food Chemistry. 2023;426:136669.
doi:10.1016/j.foodchem.2023.136669 .

Veličković, Luka, Simović, Ana, Gligorijević, Nikola, Thureau, Aurelien, Obradović, Milica, Vasović, Tamara, Sotiroudis, Georgios, Zoumpanioti, Maria, Brulet, Annie, Ćirković Veličković, Tanja, Combet, Sophie, Nikolić, Milan, Minić, Simeon, "Exploring and strengthening the potential of R-phycocyanin from Nori flakes as a food colourant" in Food Chemistry, 426 (2023):136669,
https://doi.org/10.1016/j.foodchem.2023.136669 . .

TY  - CONF
AU  - Veličković, Luka
AU  - Simović, Ana
AU  - Gligorijević, Nikola
AU  - Obradović, Milica
AU  - Sotiroudis, Georgios
AU  - Zoumpanioti, Maria
AU  - Minić, Simeon
AU  - Nikolić, Milan
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6505
AB  - Purple R-phycocyanin is a protein from red algae with the potential for application in the food industry (colorant) and wastewater treatment (binding of heavy metals). Analytical grade R-phycocyanin was purified from the buffered extract of dried Nori flakes (Porphyra spp.) by combining ammonium sulfate precipitation, hydroxyapatite, and DEAE-Sepharose column chromatography. The multimeric protein had absorption maxima characteristic for phycoerythrobilin (at 580 nm) and phycocyanobilin (at 640 nm) chromophores, high α- helical content, and melting temperature of 52°C. The secondary R-PC structure was stable under a wide range of pH values (3–9). R-phycocyanin immobilized in calcium alginate beads showed increased thermal stability and preserved antioxidant activity.
AB  - Ljubičasti R-fikocijanin je protein crvenih algi sa mogućnostima primene u industriji hrane (kolorant) i za tretman otpadnih voda (vezuje teške metale). R-fikocijanin analitičke čistoće je izolovan iz puferisanog ekstrakta osušenih Nori algi (Porphyra spp.), kombinacijom taloženja amonijum-sulfatom, hidroksiapatitne i hromatografije na DEAE-Sepharose koloni. Multimerni protein imao je apsorpcione maksimume karakteristične za fikoeritrobilinsku (na 580 nm) i fikocijanobilinsku (na 640 nm) hromoforu, visok sadržaj α-zavojnica i temperaturu topljenja od 52°C. Sekundarna struktura proteina bila je stabilna u širokom rasponu pH vrednosti (3–9). R-fikocijanin imobilisan u kuglice kalcijum-alginata pokazao je povećanu toplotnu stabilnost i očuvana antioksidativna svojstva.
PB  - Belgrade : Serbian Chemical Society
C3  - Kratki izvodi radova, knjiga radova - 59. Savetovanje Srpskog hemijskog društva, 1. i 2. jun 2023. godine, Novi Sad / Book of Abstracts, Proceedings - 59th Meeting of the Serbian Chemical Society, June 1-2, 2023, Novi Sad, Serbia
T1  - Purification and structural characterization of R-phycocyanin
T1  - Prečišćavanje i strukturna karakterizacija R-fikocijanina
SP  - 53
EP  - 53
UR  - https://hdl.handle.net/21.15107/rcub_cer_6505
ER  - 

@conference{
author = "Veličković, Luka and Simović, Ana and Gligorijević, Nikola and Obradović, Milica and Sotiroudis, Georgios and Zoumpanioti, Maria and Minić, Simeon and Nikolić, Milan",
year = "2023",
abstract = "Purple R-phycocyanin is a protein from red algae with the potential for application in the food industry (colorant) and wastewater treatment (binding of heavy metals). Analytical grade R-phycocyanin was purified from the buffered extract of dried Nori flakes (Porphyra spp.) by combining ammonium sulfate precipitation, hydroxyapatite, and DEAE-Sepharose column chromatography. The multimeric protein had absorption maxima characteristic for phycoerythrobilin (at 580 nm) and phycocyanobilin (at 640 nm) chromophores, high α- helical content, and melting temperature of 52°C. The secondary R-PC structure was stable under a wide range of pH values (3–9). R-phycocyanin immobilized in calcium alginate beads showed increased thermal stability and preserved antioxidant activity., Ljubičasti R-fikocijanin je protein crvenih algi sa mogućnostima primene u industriji hrane (kolorant) i za tretman otpadnih voda (vezuje teške metale). R-fikocijanin analitičke čistoće je izolovan iz puferisanog ekstrakta osušenih Nori algi (Porphyra spp.), kombinacijom taloženja amonijum-sulfatom, hidroksiapatitne i hromatografije na DEAE-Sepharose koloni. Multimerni protein imao je apsorpcione maksimume karakteristične za fikoeritrobilinsku (na 580 nm) i fikocijanobilinsku (na 640 nm) hromoforu, visok sadržaj α-zavojnica i temperaturu topljenja od 52°C. Sekundarna struktura proteina bila je stabilna u širokom rasponu pH vrednosti (3–9). R-fikocijanin imobilisan u kuglice kalcijum-alginata pokazao je povećanu toplotnu stabilnost i očuvana antioksidativna svojstva.",
publisher = "Belgrade : Serbian Chemical Society",
journal = "Kratki izvodi radova, knjiga radova - 59. Savetovanje Srpskog hemijskog društva, 1. i 2. jun 2023. godine, Novi Sad / Book of Abstracts, Proceedings - 59th Meeting of the Serbian Chemical Society, June 1-2, 2023, Novi Sad, Serbia",
title = "Purification and structural characterization of R-phycocyanin, Prečišćavanje i strukturna karakterizacija R-fikocijanina",
pages = "53-53",
url = "https://hdl.handle.net/21.15107/rcub_cer_6505"
}

Veličković, L., Simović, A., Gligorijević, N., Obradović, M., Sotiroudis, G., Zoumpanioti, M., Minić, S.,& Nikolić, M.. (2023). Purification and structural characterization of R-phycocyanin. in Kratki izvodi radova, knjiga radova - 59. Savetovanje Srpskog hemijskog društva, 1. i 2. jun 2023. godine, Novi Sad / Book of Abstracts, Proceedings - 59th Meeting of the Serbian Chemical Society, June 1-2, 2023, Novi Sad, Serbia
Belgrade : Serbian Chemical Society., 53-53.
https://hdl.handle.net/21.15107/rcub_cer_6505

Veličković L, Simović A, Gligorijević N, Obradović M, Sotiroudis G, Zoumpanioti M, Minić S, Nikolić M. Purification and structural characterization of R-phycocyanin. in Kratki izvodi radova, knjiga radova - 59. Savetovanje Srpskog hemijskog društva, 1. i 2. jun 2023. godine, Novi Sad / Book of Abstracts, Proceedings - 59th Meeting of the Serbian Chemical Society, June 1-2, 2023, Novi Sad, Serbia. 2023;:53-53.
https://hdl.handle.net/21.15107/rcub_cer_6505 .

Veličković, Luka, Simović, Ana, Gligorijević, Nikola, Obradović, Milica, Sotiroudis, Georgios, Zoumpanioti, Maria, Minić, Simeon, Nikolić, Milan, "Purification and structural characterization of R-phycocyanin" in Kratki izvodi radova, knjiga radova - 59. Savetovanje Srpskog hemijskog društva, 1. i 2. jun 2023. godine, Novi Sad / Book of Abstracts, Proceedings - 59th Meeting of the Serbian Chemical Society, June 1-2, 2023, Novi Sad, Serbia (2023):53-53,
https://hdl.handle.net/21.15107/rcub_cer_6505 .

TY  - CONF
AU  - Gligorijević, Nikola
AU  - Veličković, Luka
AU  - Svrzić, Nikola
AU  - Jovanović, Zorana
AU  - Minić, Simeon
AU  - Nikolić, Milan
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6519
AB  - C-Phycocyanin (C-PC), the major protein of cyanobacteria Arthrospira platensis, is a phycobiliprotein with potent biological activity. It has several beneficial effects, including anti-oxidant, anti-inflammatory, immunomodulatory, and anti-cancer. A significant challenge for the broader application of C-PC in the food industry is its stability in food processing conditions, such
as increased light exposure, temperature, and high pressure and drying. This work aimed to investigate if the immobilization of C-PC onto alginate beads could improve its stability. C-PC was
immobilized by dropping the solution of C-PC and 1% alginate (final concentration) in the solution of 2% CaCl2. Both protein/alginate mixture and CaCl2 were kept at pH 4. Immobilized CPC
was treated for 30 min at 65°C, by high pressure up to 4500 bar, and incubated under light exposure for a month. Alginate beads with immobilized C-PC were also left to dry in the fridge and kept for a month. C-PC was extracted from alginate beads by immersing them in 20 mM phosphate buffer, pH 7. The stability of C-PC was assessed by a color change and UV-VIS spectroscopy. Immobilized C-PC was stable under all tested conditions, with only small aggregation and color change appearing
after high-pressure treatment. Immobilization of C-PC by alginate thus shows promise for its efficient stabilization under food processing conditions.
PB  - Wiley
C3  - FEBS Open Bio
T1  - Stabilization of C-phycocyanin by immobilization in alginate beads
VL  - 13
IS  - S2
SP  - 234
EP  - 234
DO  - 10.1002/2211-5463.13646
ER  - 

@conference{
author = "Gligorijević, Nikola and Veličković, Luka and Svrzić, Nikola and Jovanović, Zorana and Minić, Simeon and Nikolić, Milan",
year = "2023",
abstract = "C-Phycocyanin (C-PC), the major protein of cyanobacteria Arthrospira platensis, is a phycobiliprotein with potent biological activity. It has several beneficial effects, including anti-oxidant, anti-inflammatory, immunomodulatory, and anti-cancer. A significant challenge for the broader application of C-PC in the food industry is its stability in food processing conditions, such
as increased light exposure, temperature, and high pressure and drying. This work aimed to investigate if the immobilization of C-PC onto alginate beads could improve its stability. C-PC was
immobilized by dropping the solution of C-PC and 1% alginate (final concentration) in the solution of 2% CaCl2. Both protein/alginate mixture and CaCl2 were kept at pH 4. Immobilized CPC
was treated for 30 min at 65°C, by high pressure up to 4500 bar, and incubated under light exposure for a month. Alginate beads with immobilized C-PC were also left to dry in the fridge and kept for a month. C-PC was extracted from alginate beads by immersing them in 20 mM phosphate buffer, pH 7. The stability of C-PC was assessed by a color change and UV-VIS spectroscopy. Immobilized C-PC was stable under all tested conditions, with only small aggregation and color change appearing
after high-pressure treatment. Immobilization of C-PC by alginate thus shows promise for its efficient stabilization under food processing conditions.",
publisher = "Wiley",
journal = "FEBS Open Bio",
title = "Stabilization of C-phycocyanin by immobilization in alginate beads",
volume = "13",
number = "S2",
pages = "234-234",
doi = "10.1002/2211-5463.13646"
}

Gligorijević, N., Veličković, L., Svrzić, N., Jovanović, Z., Minić, S.,& Nikolić, M.. (2023). Stabilization of C-phycocyanin by immobilization in alginate beads. in FEBS Open Bio
Wiley., 13(S2), 234-234.
https://doi.org/10.1002/2211-5463.13646

Gligorijević N, Veličković L, Svrzić N, Jovanović Z, Minić S, Nikolić M. Stabilization of C-phycocyanin by immobilization in alginate beads. in FEBS Open Bio. 2023;13(S2):234-234.
doi:10.1002/2211-5463.13646 .

Gligorijević, Nikola, Veličković, Luka, Svrzić, Nikola, Jovanović, Zorana, Minić, Simeon, Nikolić, Milan, "Stabilization of C-phycocyanin by immobilization in alginate beads" in FEBS Open Bio, 13, no. S2 (2023):234-234,
https://doi.org/10.1002/2211-5463.13646 . .

TY  - CONF
AU  - Šunderić, Miloš
AU  - Veličković, Luka
AU  - Gligorijević, Nikola
AU  - Aleksić, Ljubodrag
AU  - Nikolić, Milan
AU  - Takić, Marija
AU  - Minić, Simeon
PY  - 2023
UR  - https://euroanalysis2023.ch/
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6592
AB  - C-Phycocyanin (C-PC) is a phycobiliprotein from cyanobacteria, where it harvests light energy that is then transferred to chlorophylls during photosynthesis. It has an intense blue color due to a covalently bonded tetrapyrrole chromophore, and owing to this property is used in the food industry as a good natural alternative for food coloring. In addition to its coloring properties, C-PC has anti-inflammatory, antioxidant, anti-cancer, and immune-enhancing effects that qualify it as a dietary supplement already included in various formulations, mainly Spirulina extract powders. Since it is used as a food colorant and as a dietary supplement, it may interact with food ingredients, affecting its stability, digestibility, or antioxidant properties. Palmitic acid and linoleic acid (which can be metabolized to linolenic acid) are abundant in meat, milk, and edible oils, so that they could interact with C-PC. C-Phycocyanin isolated from the cyanobacterium Arthrospira platensis (Spirulina) was incubated with increasing concentrations of these three fatty acids, and its fluorescence intensity was monitored. Incubation resulted in a fluorescence quenching effect, indicating that binding had occurred. The binding equations indicated that the association constants were of the same order of magnitude and that the number of approximate binding sites was more than one (Ka = 4.64 x 10⁴ M-¹, n = 1.5 for linoleic acid; Ka = 2.88 x 10⁴ M–¹, n = 1.9 for linolenic acid; Ka = 0.44 x 10⁴ M–¹, n = 0.8 for palmitic acid). This moderate interaction between C-PC and fatty acids could influence its behavior as a nutraceutical and food colorant.
PB  - European Chemical Society
C3  - Euroanalysis 2023 - Analytical Probing of Complex Systems, Abstract book, August 27th - 31st, 2023, Geneva, Switzerland
T1  - Dietary fatty acids as a new binding partner of C - phycocyanin: a fluorimetric study
SP  - 332
EP  - 333
UR  - https://hdl.handle.net/21.15107/rcub_cer_6592
ER  - 

@conference{
author = "Šunderić, Miloš and Veličković, Luka and Gligorijević, Nikola and Aleksić, Ljubodrag and Nikolić, Milan and Takić, Marija and Minić, Simeon",
year = "2023",
abstract = "C-Phycocyanin (C-PC) is a phycobiliprotein from cyanobacteria, where it harvests light energy that is then transferred to chlorophylls during photosynthesis. It has an intense blue color due to a covalently bonded tetrapyrrole chromophore, and owing to this property is used in the food industry as a good natural alternative for food coloring. In addition to its coloring properties, C-PC has anti-inflammatory, antioxidant, anti-cancer, and immune-enhancing effects that qualify it as a dietary supplement already included in various formulations, mainly Spirulina extract powders. Since it is used as a food colorant and as a dietary supplement, it may interact with food ingredients, affecting its stability, digestibility, or antioxidant properties. Palmitic acid and linoleic acid (which can be metabolized to linolenic acid) are abundant in meat, milk, and edible oils, so that they could interact with C-PC. C-Phycocyanin isolated from the cyanobacterium Arthrospira platensis (Spirulina) was incubated with increasing concentrations of these three fatty acids, and its fluorescence intensity was monitored. Incubation resulted in a fluorescence quenching effect, indicating that binding had occurred. The binding equations indicated that the association constants were of the same order of magnitude and that the number of approximate binding sites was more than one (Ka = 4.64 x 10⁴ M-¹, n = 1.5 for linoleic acid; Ka = 2.88 x 10⁴ M–¹, n = 1.9 for linolenic acid; Ka = 0.44 x 10⁴ M–¹, n = 0.8 for palmitic acid). This moderate interaction between C-PC and fatty acids could influence its behavior as a nutraceutical and food colorant.",
publisher = "European Chemical Society",
journal = "Euroanalysis 2023 - Analytical Probing of Complex Systems, Abstract book, August 27th - 31st, 2023, Geneva, Switzerland",
title = "Dietary fatty acids as a new binding partner of C - phycocyanin: a fluorimetric study",
pages = "332-333",
url = "https://hdl.handle.net/21.15107/rcub_cer_6592"
}

Šunderić, M., Veličković, L., Gligorijević, N., Aleksić, L., Nikolić, M., Takić, M.,& Minić, S.. (2023). Dietary fatty acids as a new binding partner of C - phycocyanin: a fluorimetric study. in Euroanalysis 2023 - Analytical Probing of Complex Systems, Abstract book, August 27th - 31st, 2023, Geneva, Switzerland
European Chemical Society., 332-333.
https://hdl.handle.net/21.15107/rcub_cer_6592

Šunderić M, Veličković L, Gligorijević N, Aleksić L, Nikolić M, Takić M, Minić S. Dietary fatty acids as a new binding partner of C - phycocyanin: a fluorimetric study. in Euroanalysis 2023 - Analytical Probing of Complex Systems, Abstract book, August 27th - 31st, 2023, Geneva, Switzerland. 2023;:332-333.
https://hdl.handle.net/21.15107/rcub_cer_6592 .

Šunderić, Miloš, Veličković, Luka, Gligorijević, Nikola, Aleksić, Ljubodrag, Nikolić, Milan, Takić, Marija, Minić, Simeon, "Dietary fatty acids as a new binding partner of C - phycocyanin: a fluorimetric study" in Euroanalysis 2023 - Analytical Probing of Complex Systems, Abstract book, August 27th - 31st, 2023, Geneva, Switzerland (2023):332-333,
https://hdl.handle.net/21.15107/rcub_cer_6592 .

TY  - CONF
AU  - Ivanov, Aleksandar
AU  - Veličković, Luka
AU  - Jovanović, Zorana
AU  - Gligorijević, Nikola
AU  - Minić, Simeon
AU  - Nikolić, Milan
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6665
AB  - C-phycocyanin (C-PC) is a photosynthetic protein from Arthrospira platensis
(cyanobacteria). Due to its intense blue colour, which is very rare in nature, C-PC has
industrial applications as a food colourant as a substitute for synthetic food colourants.
Disadvantages of C-PC as a food colourant are its poor stability at high temperatures
(during thermal treatment of the food) and its sensibility to change pH value. The binding
of food-derived small molecules, such as vitamins, could stabilize the structure of C-PC at
high temperatures and wide pH ranges. In this study, we characterized the binding of
selected vitamins to C-PC, purified from the commercial powder of Arthrospira platensis.
We used hydrophilic vitamins (B1, B2, B7, B9, B12), lipophilic vitamins (A, D3) and
provitamin (β-carotene). Fluorescent spectroscopy showed a decrease in fluorescence of CPC
i n t he p resence o f v itamin A, v itamin D3 a nd β -carotene (lipophilic molecules)
compared to the control. In contrast, the fluorescence of C-PC in the presence of
hydrophilic vitamins showed minimal change. The protein fluorescence quenching
approach demonstrated hydrophobic (pro)vitamins binding affinities ranging from 0.02 to
5.9 x 105 M-1, with the ability of hydrophobic (pro)vitamins to bind at the different sites on
C-PC. UV-VIS spectrophotometry showed that the binding of hydrophobic (pro)vitamins
does not affect the protein colour, while CD spectroscopy revealed that the binding of
chosen molecules does not significantly influence the secondary structure of C-PC.
Overall, this study demonstrated C-PC's significant potential in binding hydrophobic
(pro)vitamins, while further research is required to test if these ligands could improve CPC
stability.
PB  - Serbian Biochemical Society
C3  - Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia
T1  - Examination of C-phycocyanin interactions with selected vitamins
SP  - 106
EP  - 106
UR  - https://hdl.handle.net/21.15107/rcub_cer_6665
ER  - 

@conference{
author = "Ivanov, Aleksandar and Veličković, Luka and Jovanović, Zorana and Gligorijević, Nikola and Minić, Simeon and Nikolić, Milan",
year = "2023",
abstract = "C-phycocyanin (C-PC) is a photosynthetic protein from Arthrospira platensis
(cyanobacteria). Due to its intense blue colour, which is very rare in nature, C-PC has
industrial applications as a food colourant as a substitute for synthetic food colourants.
Disadvantages of C-PC as a food colourant are its poor stability at high temperatures
(during thermal treatment of the food) and its sensibility to change pH value. The binding
of food-derived small molecules, such as vitamins, could stabilize the structure of C-PC at
high temperatures and wide pH ranges. In this study, we characterized the binding of
selected vitamins to C-PC, purified from the commercial powder of Arthrospira platensis.
We used hydrophilic vitamins (B1, B2, B7, B9, B12), lipophilic vitamins (A, D3) and
provitamin (β-carotene). Fluorescent spectroscopy showed a decrease in fluorescence of CPC
i n t he p resence o f v itamin A, v itamin D3 a nd β -carotene (lipophilic molecules)
compared to the control. In contrast, the fluorescence of C-PC in the presence of
hydrophilic vitamins showed minimal change. The protein fluorescence quenching
approach demonstrated hydrophobic (pro)vitamins binding affinities ranging from 0.02 to
5.9 x 105 M-1, with the ability of hydrophobic (pro)vitamins to bind at the different sites on
C-PC. UV-VIS spectrophotometry showed that the binding of hydrophobic (pro)vitamins
does not affect the protein colour, while CD spectroscopy revealed that the binding of
chosen molecules does not significantly influence the secondary structure of C-PC.
Overall, this study demonstrated C-PC's significant potential in binding hydrophobic
(pro)vitamins, while further research is required to test if these ligands could improve CPC
stability.",
publisher = "Serbian Biochemical Society",
journal = "Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia",
title = "Examination of C-phycocyanin interactions with selected vitamins",
pages = "106-106",
url = "https://hdl.handle.net/21.15107/rcub_cer_6665"
}

Ivanov, A., Veličković, L., Jovanović, Z., Gligorijević, N., Minić, S.,& Nikolić, M.. (2023). Examination of C-phycocyanin interactions with selected vitamins. in Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia
Serbian Biochemical Society., 106-106.
https://hdl.handle.net/21.15107/rcub_cer_6665

Ivanov A, Veličković L, Jovanović Z, Gligorijević N, Minić S, Nikolić M. Examination of C-phycocyanin interactions with selected vitamins. in Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia. 2023;:106-106.
https://hdl.handle.net/21.15107/rcub_cer_6665 .

Ivanov, Aleksandar, Veličković, Luka, Jovanović, Zorana, Gligorijević, Nikola, Minić, Simeon, Nikolić, Milan, "Examination of C-phycocyanin interactions with selected vitamins" in Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia (2023):106-106,
https://hdl.handle.net/21.15107/rcub_cer_6665 .

TY  - CONF
AU  - Aleksić, Ljubodrag
AU  - Veličković, Luka
AU  - Gligorijević, Nikola
AU  - Šunderić, Miloš
AU  - Takić, Marija
AU  - Nikolić, Milan
AU  - Minić, Simeon
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6667
AB  - Cultured meat requires less land and water and is less polluting, but still costly. The critical
challenge in cultivated meat science is identifying and developing bovine serum albumin
alternatives as the key component in cell media. Phycobiliproteins (PBPs) from micro- and
macroalgae are promising candidates for albumin replacement due to their high abundance
and well-known excellent antioxidative and metal-binding activities of covalently attached
tetrapyrrole chromophores. Considering the importance of fatty acids (FA) binding by
albumin for cell cultivation, the additional prerequisites for developing PBPs as albumin
replacement components is their validation for the ability to bind FA. This study aims to
examine the ability of C-phycocyanin (C-PC), the major PBP of microalgae Arthrospira
platensis, to bind seven fatty acids (stearic, palmitic, oleic, elaidic, linoleic, linolenic and
docosahexaenoic acid). For this purpose, we employed various optical spectroscopy
techniques (fluorescence, CD, and VIS absorption spectroscopy). The protein fluorescence
quenching approach demonstrated FA binding affinities ranging from 0.42 to 2.4 x 105
M−1, with the ability of FA to bind at different sites on C-PC. Fatty acid binding induces
substantial changes in the VIS absorption spectra of C-PC, indicating the FA are attached
in the vicinity of C-PC chromophores. On the other hand, CD spectroscopy did not show
significant effects of FA binding on C-PC secondary structure content. Overall, this study
revealed C-PC's significant potential in binding FA, the critical prerequisite to replacing
albumin for developing animal-free cell media for meat cultivation.
PB  - Serbian Biochemical Society
C3  - Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia
T1  - Examining fatty acid interactions with Arthrospira platensis-derived C-phycocyanin
SP  - 121
EP  - 121
UR  - https://hdl.handle.net/21.15107/rcub_cer_6667
ER  - 

@conference{
author = "Aleksić, Ljubodrag and Veličković, Luka and Gligorijević, Nikola and Šunderić, Miloš and Takić, Marija and Nikolić, Milan and Minić, Simeon",
year = "2023",
abstract = "Cultured meat requires less land and water and is less polluting, but still costly. The critical
challenge in cultivated meat science is identifying and developing bovine serum albumin
alternatives as the key component in cell media. Phycobiliproteins (PBPs) from micro- and
macroalgae are promising candidates for albumin replacement due to their high abundance
and well-known excellent antioxidative and metal-binding activities of covalently attached
tetrapyrrole chromophores. Considering the importance of fatty acids (FA) binding by
albumin for cell cultivation, the additional prerequisites for developing PBPs as albumin
replacement components is their validation for the ability to bind FA. This study aims to
examine the ability of C-phycocyanin (C-PC), the major PBP of microalgae Arthrospira
platensis, to bind seven fatty acids (stearic, palmitic, oleic, elaidic, linoleic, linolenic and
docosahexaenoic acid). For this purpose, we employed various optical spectroscopy
techniques (fluorescence, CD, and VIS absorption spectroscopy). The protein fluorescence
quenching approach demonstrated FA binding affinities ranging from 0.42 to 2.4 x 105
M−1, with the ability of FA to bind at different sites on C-PC. Fatty acid binding induces
substantial changes in the VIS absorption spectra of C-PC, indicating the FA are attached
in the vicinity of C-PC chromophores. On the other hand, CD spectroscopy did not show
significant effects of FA binding on C-PC secondary structure content. Overall, this study
revealed C-PC's significant potential in binding FA, the critical prerequisite to replacing
albumin for developing animal-free cell media for meat cultivation.",
publisher = "Serbian Biochemical Society",
journal = "Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia",
title = "Examining fatty acid interactions with Arthrospira platensis-derived C-phycocyanin",
pages = "121-121",
url = "https://hdl.handle.net/21.15107/rcub_cer_6667"
}

Aleksić, L., Veličković, L., Gligorijević, N., Šunderić, M., Takić, M., Nikolić, M.,& Minić, S.. (2023). Examining fatty acid interactions with Arthrospira platensis-derived C-phycocyanin. in Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia
Serbian Biochemical Society., 121-121.
https://hdl.handle.net/21.15107/rcub_cer_6667

Aleksić L, Veličković L, Gligorijević N, Šunderić M, Takić M, Nikolić M, Minić S. Examining fatty acid interactions with Arthrospira platensis-derived C-phycocyanin. in Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia. 2023;:121-121.
https://hdl.handle.net/21.15107/rcub_cer_6667 .

Aleksić, Ljubodrag, Veličković, Luka, Gligorijević, Nikola, Šunderić, Miloš, Takić, Marija, Nikolić, Milan, Minić, Simeon, "Examining fatty acid interactions with Arthrospira platensis-derived C-phycocyanin" in Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia (2023):121-121,
https://hdl.handle.net/21.15107/rcub_cer_6667 .

TY  - CONF
AU  - Jovanović, Zorana
AU  - Annighöfer, Burkhard
AU  - Dudzinski, Daniel
AU  - Veličković, Luka
AU  - Gligorijević, Nikola
AU  - Nikolić, Milan
AU  - Brûlet, Annie
AU  - Assifaoui, Ali
AU  - Combet, Sophie
AU  - Minić, Simeon
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6669
AB  - The color of food products is an important aspect in food industry, and its preservation
remains a big challenge. We aim to preserve the natural blue dye of C-phycocyanin (C-PC)
phycobiliprotein from Spirulina microalgae. For this purpose, we incorporated C-PC in
combined starch and β-lactoglobulin (BLG) hydrogels by using a high-pressure (HP)
process. Indeed, in thermal treatment, the color derived from C-PC is entirely lost. We
characterized the obtained HP gels by both rheology and small-angle X-ray scattering
(SAXS). Various formulations of binary (BLG/C-PC) and ternary (starch/BLG/C-PC)
systems were tested under HP up to 4,500 bar. A good preservation of the C-PC pigment
was established by mixing BLG and starch with C-PC at pH 7, with concentrations of 180,
5, and 10 mg/mL, respectively. Identical component concentrations were maintained in the
binary systems. Structure of gels was characterized by SAXS providing insight of C-PC
interactions with BLG and starch after HP process which leads to the formation of solid
gels with larger mesh compared to two-component systems. This results in enhanced
mechanical properties, which were determined by amplitude and frequency sweep
measurements using a rheometer with applied plane/plane geometry. Therefore, adding
starch, even at small concentration, significantly improves gel visual appearance and
mechanical properties. Our study reveals that preservation through HP treatment is more
effective than high temperature treatment, as visually observed through the sustained color
integrity of C-PC blue dye.
PB  - Serbian Biochemical Society
C3  - Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia
T1  - Combined hydrogels of starch and β-lactoglobulin as matrices for the preservation of C-phycocyanin
SP  - 150
EP  - 150
UR  - https://hdl.handle.net/21.15107/rcub_cer_6669
ER  - 

@conference{
author = "Jovanović, Zorana and Annighöfer, Burkhard and Dudzinski, Daniel and Veličković, Luka and Gligorijević, Nikola and Nikolić, Milan and Brûlet, Annie and Assifaoui, Ali and Combet, Sophie and Minić, Simeon",
year = "2023",
abstract = "The color of food products is an important aspect in food industry, and its preservation
remains a big challenge. We aim to preserve the natural blue dye of C-phycocyanin (C-PC)
phycobiliprotein from Spirulina microalgae. For this purpose, we incorporated C-PC in
combined starch and β-lactoglobulin (BLG) hydrogels by using a high-pressure (HP)
process. Indeed, in thermal treatment, the color derived from C-PC is entirely lost. We
characterized the obtained HP gels by both rheology and small-angle X-ray scattering
(SAXS). Various formulations of binary (BLG/C-PC) and ternary (starch/BLG/C-PC)
systems were tested under HP up to 4,500 bar. A good preservation of the C-PC pigment
was established by mixing BLG and starch with C-PC at pH 7, with concentrations of 180,
5, and 10 mg/mL, respectively. Identical component concentrations were maintained in the
binary systems. Structure of gels was characterized by SAXS providing insight of C-PC
interactions with BLG and starch after HP process which leads to the formation of solid
gels with larger mesh compared to two-component systems. This results in enhanced
mechanical properties, which were determined by amplitude and frequency sweep
measurements using a rheometer with applied plane/plane geometry. Therefore, adding
starch, even at small concentration, significantly improves gel visual appearance and
mechanical properties. Our study reveals that preservation through HP treatment is more
effective than high temperature treatment, as visually observed through the sustained color
integrity of C-PC blue dye.",
publisher = "Serbian Biochemical Society",
journal = "Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia",
title = "Combined hydrogels of starch and β-lactoglobulin as matrices for the preservation of C-phycocyanin",
pages = "150-150",
url = "https://hdl.handle.net/21.15107/rcub_cer_6669"
}

Jovanović, Z., Annighöfer, B., Dudzinski, D., Veličković, L., Gligorijević, N., Nikolić, M., Brûlet, A., Assifaoui, A., Combet, S.,& Minić, S.. (2023). Combined hydrogels of starch and β-lactoglobulin as matrices for the preservation of C-phycocyanin. in Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia
Serbian Biochemical Society., 150-150.
https://hdl.handle.net/21.15107/rcub_cer_6669

Jovanović Z, Annighöfer B, Dudzinski D, Veličković L, Gligorijević N, Nikolić M, Brûlet A, Assifaoui A, Combet S, Minić S. Combined hydrogels of starch and β-lactoglobulin as matrices for the preservation of C-phycocyanin. in Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia. 2023;:150-150.
https://hdl.handle.net/21.15107/rcub_cer_6669 .

Jovanović, Zorana, Annighöfer, Burkhard, Dudzinski, Daniel, Veličković, Luka, Gligorijević, Nikola, Nikolić, Milan, Brûlet, Annie, Assifaoui, Ali, Combet, Sophie, Minić, Simeon, "Combined hydrogels of starch and β-lactoglobulin as matrices for the preservation of C-phycocyanin" in Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia (2023):150-150,
https://hdl.handle.net/21.15107/rcub_cer_6669 .