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  - 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  - 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 .