TY  - CONF
AU  - Stefanović, Marija
AU  - Savić, Aleksa
AU  - Božić, Nataša
AU  - Vujčić, Zoran
AU  - Radosavljević, Jelena
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/7345
AB  - Viral exonucleases play role in many processes essential for genome ma intenance,including DNA repair and recombination. Lambda exonuclease (λ -exo), isolated fromlambda bacteriophage, hydrolases double-stranded DNA (dsDNA) in the highly processivemanner in 5’→3’ direction, yielding mononucleotides and single -stranded DNA (ssDNA).This unique enzymatic properties offer several promising biotechnological applications,such as highly sensitive quantification of DNA modifications and single -moleculesequencing. Hence, optimization of the expression conditions is a prerequisite to achievehigh-level production of λ-exo. Here we have tested λ -exo expression in five different E.coli strains under various temperature regimes in order to establish the optimal conditionsfor efficient production of recombinant λ -exo. The N-terminally His -tagged λ-exo wassuccessfully expressed in E.coli BL21(AI), SHuffle T7, C41(DE3) and C43(DE3) strains inLB broth. Collected aliquots were analysed by SDS-PAGE, followed by CBB staining.Relative yield of target protein bands was determined by densitometry in total cell lysate, aswell as in soluble and insoluble cytoplasmatic fractions. We identified E.coli BL21(AI),SHuffle T7 and C41(DE3) as good producers of recombinant λ -exo, and upon scaling up, λ-exo was purified from crude cell lysates by metal affinity chromatography in satisfactoryyield. Our data suggest that densitometric analysis could serve as a powerful low-costscreening platform for improving recombinant protein expression strategies.
PB  - Prirodno-matematički fakultet, Univerzitet u Kragujevcu
C3  - Zbornik apstrakata, VI Simpozijum Srpskog udruženja za proteomiku (SePA) “Razvoj i primena novih metoda proteomike”, 2. jun 2023. godine, Kragujevac
T1  - Electrophoretic assessment of recombinant λ- exonuclease production in different E. coli strains
SP  - 23
EP  - 23
UR  - https://hdl.handle.net/21.15107/rcub_cer_7345
ER  - 

@conference{
author = "Stefanović, Marija and Savić, Aleksa and Božić, Nataša and Vujčić, Zoran and Radosavljević, Jelena",
year = "2023",
abstract = "Viral exonucleases play role in many processes essential for genome ma intenance,including DNA repair and recombination. Lambda exonuclease (λ -exo), isolated fromlambda bacteriophage, hydrolases double-stranded DNA (dsDNA) in the highly processivemanner in 5’→3’ direction, yielding mononucleotides and single -stranded DNA (ssDNA).This unique enzymatic properties offer several promising biotechnological applications,such as highly sensitive quantification of DNA modifications and single -moleculesequencing. Hence, optimization of the expression conditions is a prerequisite to achievehigh-level production of λ-exo. Here we have tested λ -exo expression in five different E.coli strains under various temperature regimes in order to establish the optimal conditionsfor efficient production of recombinant λ -exo. The N-terminally His -tagged λ-exo wassuccessfully expressed in E.coli BL21(AI), SHuffle T7, C41(DE3) and C43(DE3) strains inLB broth. Collected aliquots were analysed by SDS-PAGE, followed by CBB staining.Relative yield of target protein bands was determined by densitometry in total cell lysate, aswell as in soluble and insoluble cytoplasmatic fractions. We identified E.coli BL21(AI),SHuffle T7 and C41(DE3) as good producers of recombinant λ -exo, and upon scaling up, λ-exo was purified from crude cell lysates by metal affinity chromatography in satisfactoryyield. Our data suggest that densitometric analysis could serve as a powerful low-costscreening platform for improving recombinant protein expression strategies.",
publisher = "Prirodno-matematički fakultet, Univerzitet u Kragujevcu",
journal = "Zbornik apstrakata, VI Simpozijum Srpskog udruženja za proteomiku (SePA) “Razvoj i primena novih metoda proteomike”, 2. jun 2023. godine, Kragujevac",
title = "Electrophoretic assessment of recombinant λ- exonuclease production in different E. coli strains",
pages = "23-23",
url = "https://hdl.handle.net/21.15107/rcub_cer_7345"
}

Stefanović, M., Savić, A., Božić, N., Vujčić, Z.,& Radosavljević, J.. (2023). Electrophoretic assessment of recombinant λ- exonuclease production in different E. coli strains. in Zbornik apstrakata, VI Simpozijum Srpskog udruženja za proteomiku (SePA) “Razvoj i primena novih metoda proteomike”, 2. jun 2023. godine, Kragujevac
Prirodno-matematički fakultet, Univerzitet u Kragujevcu., 23-23.
https://hdl.handle.net/21.15107/rcub_cer_7345

Stefanović M, Savić A, Božić N, Vujčić Z, Radosavljević J. Electrophoretic assessment of recombinant λ- exonuclease production in different E. coli strains. in Zbornik apstrakata, VI Simpozijum Srpskog udruženja za proteomiku (SePA) “Razvoj i primena novih metoda proteomike”, 2. jun 2023. godine, Kragujevac. 2023;:23-23.
https://hdl.handle.net/21.15107/rcub_cer_7345 .

Stefanović, Marija, Savić, Aleksa, Božić, Nataša, Vujčić, Zoran, Radosavljević, Jelena, "Electrophoretic assessment of recombinant λ- exonuclease production in different E. coli strains" in Zbornik apstrakata, VI Simpozijum Srpskog udruženja za proteomiku (SePA) “Razvoj i primena novih metoda proteomike”, 2. jun 2023. godine, Kragujevac (2023):23-23,
https://hdl.handle.net/21.15107/rcub_cer_7345 .

TY  - CONF
AU  - Stefanović, Marija
AU  - Savić, Aleksa
AU  - Božić, Nataša
AU  - Vujčić, Zoran
AU  - Radosavljević, Jelena
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/7346
AB  - Viral exonucleases play role in many processes essential for genome ma intenance,including DNA repair and recombination. Lambda exonuclease (λ -exo), isolated fromlambda bacteriophage, hydrolases double-stranded DNA (dsDNA) in the highly processivemanner in 5’→3’ direction, yielding mononucleotides and single -stranded DNA (ssDNA).This unique enzymatic properties offer several promising biotechnological applications,such as highly sensitive quantification of DNA modifications and single -moleculesequencing. Hence, optimization of the expression conditions is a prerequisite to achievehigh-level production of λ-exo. Here we have tested λ -exo expression in five different E.coli strains under various temperature regimes in order to establish the optimal conditionsfor efficient production of recombinant λ -exo. The N-terminally His -tagged λ-exo wassuccessfully expressed in E.coli BL21(AI), SHuffle T7, C41(DE3) and C43(DE3) strains inLB broth. Collected aliquots were analysed by SDS-PAGE, followed by CBB staining.Relative yield of target protein bands was determined by densitometry in total cell lysate, aswell as in soluble and insoluble cytoplasmatic fractions. We identified E.coli BL21(AI),SHuffle T7 and C41(DE3) as good producers of recombinant λ -exo, and upon scaling up, λ-exo was purified from crude cell lysates by metal affinity chromatography in satisfactoryyield. Our data suggest that densitometric analysis could serve as a powerful low-costscreening platform for improving recombinant protein expression strategies.
PB  - Prirodno-matematički fakultet, Univerzitet u Kragujevcu
T1  - Poster presentation: Electrophoretic assessment of recombinant λ- exonuclease production in different E. coli strains
UR  - https://hdl.handle.net/21.15107/rcub_cer_7346
ER  - 

@conference{
author = "Stefanović, Marija and Savić, Aleksa and Božić, Nataša and Vujčić, Zoran and Radosavljević, Jelena",
year = "2023",
abstract = "Viral exonucleases play role in many processes essential for genome ma intenance,including DNA repair and recombination. Lambda exonuclease (λ -exo), isolated fromlambda bacteriophage, hydrolases double-stranded DNA (dsDNA) in the highly processivemanner in 5’→3’ direction, yielding mononucleotides and single -stranded DNA (ssDNA).This unique enzymatic properties offer several promising biotechnological applications,such as highly sensitive quantification of DNA modifications and single -moleculesequencing. Hence, optimization of the expression conditions is a prerequisite to achievehigh-level production of λ-exo. Here we have tested λ -exo expression in five different E.coli strains under various temperature regimes in order to establish the optimal conditionsfor efficient production of recombinant λ -exo. The N-terminally His -tagged λ-exo wassuccessfully expressed in E.coli BL21(AI), SHuffle T7, C41(DE3) and C43(DE3) strains inLB broth. Collected aliquots were analysed by SDS-PAGE, followed by CBB staining.Relative yield of target protein bands was determined by densitometry in total cell lysate, aswell as in soluble and insoluble cytoplasmatic fractions. We identified E.coli BL21(AI),SHuffle T7 and C41(DE3) as good producers of recombinant λ -exo, and upon scaling up, λ-exo was purified from crude cell lysates by metal affinity chromatography in satisfactoryyield. Our data suggest that densitometric analysis could serve as a powerful low-costscreening platform for improving recombinant protein expression strategies.",
publisher = "Prirodno-matematički fakultet, Univerzitet u Kragujevcu",
title = "Poster presentation: Electrophoretic assessment of recombinant λ- exonuclease production in different E. coli strains",
url = "https://hdl.handle.net/21.15107/rcub_cer_7346"
}

Stefanović, M., Savić, A., Božić, N., Vujčić, Z.,& Radosavljević, J.. (2023). Poster presentation: Electrophoretic assessment of recombinant λ- exonuclease production in different E. coli strains. 
Prirodno-matematički fakultet, Univerzitet u Kragujevcu..
https://hdl.handle.net/21.15107/rcub_cer_7346

Stefanović M, Savić A, Božić N, Vujčić Z, Radosavljević J. Poster presentation: Electrophoretic assessment of recombinant λ- exonuclease production in different E. coli strains. 2023;.
https://hdl.handle.net/21.15107/rcub_cer_7346 .

Stefanović, Marija, Savić, Aleksa, Božić, Nataša, Vujčić, Zoran, Radosavljević, Jelena, "Poster presentation: Electrophoretic assessment of recombinant λ- exonuclease production in different E. coli strains" (2023),
https://hdl.handle.net/21.15107/rcub_cer_7346 .

TY  - JOUR
AU  - Radosavljević, Jelena
AU  - Stanić-Vučinić, Dragana
AU  - Stojadinović, Marija M.
AU  - Radomirović, Mirjana Ž.
AU  - Simović, Ana
AU  - Radibratović, Milica
AU  - Ćirković-Veličković, Tanja
PY  - 2022
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/5555
AB  - Background: The world’s production of whey is estimated to be more than 200 milliontons per year. Although whey is an important source of proteins with high nutritional value andbiotechnological importance, it is still considered as a by-product of the dairy industry with loweconomic value due to low industrial exploitation. There are several challenges in the separation ofwhey proteins: low concentration, the complexity of the material and similar properties (pI, molecularmass) of some proteins.Methods: A narrative review of all the relevant papers on the present methodologies based on ionexchange and adsorption principles for isolation of whey proteins, known to the authors, was conductedResults: Traditional ion exchange techniques are widely used for the separation and purification ofthe bovine whey proteins. These methodologies, based on the anion or cation chromatographicprocedures, as well as the combination of aforementioned techniques are still preferential methodsfor the isolation of the whey proteins on the laboratory scale. However, more recent research on ionexchange membranes for this purpose has been introduced, with promising potential to be appliedon the pilot industrial scale. Newly developed methodologies based either on the ion exchangeseparation (for example: simulated moving bed chromatography, expanded bed adsorption, magneticion exchangers, etc.) or adsorption (for example: adsorption on hydroxyapatite or activatedcarbon, or molecular imprinting) are promising approaches for scaling up of the whey proteins’purification processes.Conclusion: Many procedures based on ion exchange are successfully implemented for the separationand purification of whey proteins, providing protein preparations of moderate-to-high yieldand satisfactory purity. However, the authors anticipate further development of adsorption-basedmethodologies for the separation of whey proteins by targeting the differences in proteins’ structuresrather than targeting the differences in molecular masses and pI. The complex composite multilayeredmatrices, including also inorganic components, are promising materials for simultaneousexploiting of the differences in the masses, pI and structures of whey proteins for the separation.
PB  - Bentham Science
T2  - Current Analytical Chemistry
T1  - Application of Ion Exchange and Adsorption Techniques for Separation of Whey Proteins from Bovine Milk
VL  - 18
IS  - 3
SP  - 341
EP  - 359
DO  - 10.2174/1573411017666210108092338
ER  - 

@article{
author = "Radosavljević, Jelena and Stanić-Vučinić, Dragana and Stojadinović, Marija M. and Radomirović, Mirjana Ž. and Simović, Ana and Radibratović, Milica and Ćirković-Veličković, Tanja",
year = "2022",
abstract = "Background: The world’s production of whey is estimated to be more than 200 milliontons per year. Although whey is an important source of proteins with high nutritional value andbiotechnological importance, it is still considered as a by-product of the dairy industry with loweconomic value due to low industrial exploitation. There are several challenges in the separation ofwhey proteins: low concentration, the complexity of the material and similar properties (pI, molecularmass) of some proteins.Methods: A narrative review of all the relevant papers on the present methodologies based on ionexchange and adsorption principles for isolation of whey proteins, known to the authors, was conductedResults: Traditional ion exchange techniques are widely used for the separation and purification ofthe bovine whey proteins. These methodologies, based on the anion or cation chromatographicprocedures, as well as the combination of aforementioned techniques are still preferential methodsfor the isolation of the whey proteins on the laboratory scale. However, more recent research on ionexchange membranes for this purpose has been introduced, with promising potential to be appliedon the pilot industrial scale. Newly developed methodologies based either on the ion exchangeseparation (for example: simulated moving bed chromatography, expanded bed adsorption, magneticion exchangers, etc.) or adsorption (for example: adsorption on hydroxyapatite or activatedcarbon, or molecular imprinting) are promising approaches for scaling up of the whey proteins’purification processes.Conclusion: Many procedures based on ion exchange are successfully implemented for the separationand purification of whey proteins, providing protein preparations of moderate-to-high yieldand satisfactory purity. However, the authors anticipate further development of adsorption-basedmethodologies for the separation of whey proteins by targeting the differences in proteins’ structuresrather than targeting the differences in molecular masses and pI. The complex composite multilayeredmatrices, including also inorganic components, are promising materials for simultaneousexploiting of the differences in the masses, pI and structures of whey proteins for the separation.",
publisher = "Bentham Science",
journal = "Current Analytical Chemistry",
title = "Application of Ion Exchange and Adsorption Techniques for Separation of Whey Proteins from Bovine Milk",
volume = "18",
number = "3",
pages = "341-359",
doi = "10.2174/1573411017666210108092338"
}

Radosavljević, J., Stanić-Vučinić, D., Stojadinović, M. M., Radomirović, M. Ž., Simović, A., Radibratović, M.,& Ćirković-Veličković, T.. (2022). Application of Ion Exchange and Adsorption Techniques for Separation of Whey Proteins from Bovine Milk. in Current Analytical Chemistry
Bentham Science., 18(3), 341-359.
https://doi.org/10.2174/1573411017666210108092338

Radosavljević J, Stanić-Vučinić D, Stojadinović MM, Radomirović MŽ, Simović A, Radibratović M, Ćirković-Veličković T. Application of Ion Exchange and Adsorption Techniques for Separation of Whey Proteins from Bovine Milk. in Current Analytical Chemistry. 2022;18(3):341-359.
doi:10.2174/1573411017666210108092338 .

Radosavljević, Jelena, Stanić-Vučinić, Dragana, Stojadinović, Marija M., Radomirović, Mirjana Ž., Simović, Ana, Radibratović, Milica, Ćirković-Veličković, Tanja, "Application of Ion Exchange and Adsorption Techniques for Separation of Whey Proteins from Bovine Milk" in Current Analytical Chemistry, 18, no. 3 (2022):341-359,
https://doi.org/10.2174/1573411017666210108092338 . .

TY  - JOUR
AU  - Radosavljević, Jelena
AU  - Stanić-Vučinić, Dragana
AU  - Stojadinović, Marija M.
AU  - Radomirović, Mirjana Ž.
AU  - Simović, Ana
AU  - Radibratović, Milica
AU  - Ćirković-Veličković, Tanja
PY  - 2022
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/5556
AB  - Background: The world’s production of whey is estimated to be more than 200 milliontons per year. Although whey is an important source of proteins with high nutritional value andbiotechnological importance, it is still considered as a by-product of the dairy industry with loweconomic value due to low industrial exploitation. There are several challenges in the separation ofwhey proteins: low concentration, the complexity of the material and similar properties (pI, molecularmass) of some proteins.Methods: A narrative review of all the relevant papers on the present methodologies based on ionexchange and adsorption principles for isolation of whey proteins, known to the authors, was conductedResults: Traditional ion exchange techniques are widely used for the separation and purification ofthe bovine whey proteins. These methodologies, based on the anion or cation chromatographicprocedures, as well as the combination of aforementioned techniques are still preferential methodsfor the isolation of the whey proteins on the laboratory scale. However, more recent research on ionexchange membranes for this purpose has been introduced, with promising potential to be appliedon the pilot industrial scale. Newly developed methodologies based either on the ion exchangeseparation (for example: simulated moving bed chromatography, expanded bed adsorption, magneticion exchangers, etc.) or adsorption (for example: adsorption on hydroxyapatite or activatedcarbon, or molecular imprinting) are promising approaches for scaling up of the whey proteins’purification processes.Conclusion: Many procedures based on ion exchange are successfully implemented for the separationand purification of whey proteins, providing protein preparations of moderate-to-high yieldand satisfactory purity. However, the authors anticipate further development of adsorption-basedmethodologies for the separation of whey proteins by targeting the differences in proteins’ structuresrather than targeting the differences in molecular masses and pI. The complex composite multilayeredmatrices, including also inorganic components, are promising materials for simultaneousexploiting of the differences in the masses, pI and structures of whey proteins for the separation.
PB  - Bentham Science
T2  - Current Analytical Chemistry
T1  - Application of Ion Exchange and Adsorption Techniques for Separation of Whey Proteins from Bovine Milk
VL  - 18
IS  - 3
SP  - 341
EP  - 359
DO  - 10.2174/1573411017666210108092338
ER  - 

@article{
author = "Radosavljević, Jelena and Stanić-Vučinić, Dragana and Stojadinović, Marija M. and Radomirović, Mirjana Ž. and Simović, Ana and Radibratović, Milica and Ćirković-Veličković, Tanja",
year = "2022",
abstract = "Background: The world’s production of whey is estimated to be more than 200 milliontons per year. Although whey is an important source of proteins with high nutritional value andbiotechnological importance, it is still considered as a by-product of the dairy industry with loweconomic value due to low industrial exploitation. There are several challenges in the separation ofwhey proteins: low concentration, the complexity of the material and similar properties (pI, molecularmass) of some proteins.Methods: A narrative review of all the relevant papers on the present methodologies based on ionexchange and adsorption principles for isolation of whey proteins, known to the authors, was conductedResults: Traditional ion exchange techniques are widely used for the separation and purification ofthe bovine whey proteins. These methodologies, based on the anion or cation chromatographicprocedures, as well as the combination of aforementioned techniques are still preferential methodsfor the isolation of the whey proteins on the laboratory scale. However, more recent research on ionexchange membranes for this purpose has been introduced, with promising potential to be appliedon the pilot industrial scale. Newly developed methodologies based either on the ion exchangeseparation (for example: simulated moving bed chromatography, expanded bed adsorption, magneticion exchangers, etc.) or adsorption (for example: adsorption on hydroxyapatite or activatedcarbon, or molecular imprinting) are promising approaches for scaling up of the whey proteins’purification processes.Conclusion: Many procedures based on ion exchange are successfully implemented for the separationand purification of whey proteins, providing protein preparations of moderate-to-high yieldand satisfactory purity. However, the authors anticipate further development of adsorption-basedmethodologies for the separation of whey proteins by targeting the differences in proteins’ structuresrather than targeting the differences in molecular masses and pI. The complex composite multilayeredmatrices, including also inorganic components, are promising materials for simultaneousexploiting of the differences in the masses, pI and structures of whey proteins for the separation.",
publisher = "Bentham Science",
journal = "Current Analytical Chemistry",
title = "Application of Ion Exchange and Adsorption Techniques for Separation of Whey Proteins from Bovine Milk",
volume = "18",
number = "3",
pages = "341-359",
doi = "10.2174/1573411017666210108092338"
}

Radosavljević, J., Stanić-Vučinić, D., Stojadinović, M. M., Radomirović, M. Ž., Simović, A., Radibratović, M.,& Ćirković-Veličković, T.. (2022). Application of Ion Exchange and Adsorption Techniques for Separation of Whey Proteins from Bovine Milk. in Current Analytical Chemistry
Bentham Science., 18(3), 341-359.
https://doi.org/10.2174/1573411017666210108092338

Radosavljević J, Stanić-Vučinić D, Stojadinović MM, Radomirović MŽ, Simović A, Radibratović M, Ćirković-Veličković T. Application of Ion Exchange and Adsorption Techniques for Separation of Whey Proteins from Bovine Milk. in Current Analytical Chemistry. 2022;18(3):341-359.
doi:10.2174/1573411017666210108092338 .

Radosavljević, Jelena, Stanić-Vučinić, Dragana, Stojadinović, Marija M., Radomirović, Mirjana Ž., Simović, Ana, Radibratović, Milica, Ćirković-Veličković, Tanja, "Application of Ion Exchange and Adsorption Techniques for Separation of Whey Proteins from Bovine Milk" in Current Analytical Chemistry, 18, no. 3 (2022):341-359,
https://doi.org/10.2174/1573411017666210108092338 . .

TY  - JOUR
AU  - Anđelković, Ljubica
AU  - Jeremić, Dejan
AU  - Milenković, Milica R.
AU  - Radosavljević, Jelena
AU  - Vulić, Predrag
AU  - Pavlović, Vladimir B.
AU  - Manojlović, Dragan
AU  - Nikolić, Aleksandar S.
PY  - 2020
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/3145
AB  - A simple organic-phase synthesis process was used to produce bare NiFe2O4 and ZnFe2O4 and core-shell ZnFe2O4@NiFe2O4 ferrite nanoparticles. X-ray powder diffractograms for all investigated powders show characteristic peaks of a spinel cubic structure without a secondary phase. Transmission electron microscopy (TEM) indicated the presence of nanoparticles that are smaller than 20 nm. The release of divalent ions (Ni2+ and Zn2+) from synthesized nanoparticles that were dispersed in saline solution, phosphate-buffered saline (PBS) and human serum, as determined by the inductively coupled plasma mass spectrometry (ICP-MS) method, was lower than 2 wt %. These results demonstrate the stability of the investigated nanoparticles in biologically relevant media and exclude the toxicity of Ni2+ and Zn2+ due to metal ion release, thereby opening a broad range of (bio)medical applications.
PB  - Elsevier
T2  - Ceramics International
T1  - Synthesis, characterization and in vitro evaluation of divalent ion release from stable NiFe2O4, ZnFe2O4 and core-shell ZnFe2O4@NiFe2O4 nanoparticles
VL  - 46
IS  - 3
SP  - 3528
EP  - 3533
DO  - 10.1016/j.ceramint.2019.10.068
ER  - 

@article{
author = "Anđelković, Ljubica and Jeremić, Dejan and Milenković, Milica R. and Radosavljević, Jelena and Vulić, Predrag and Pavlović, Vladimir B. and Manojlović, Dragan and Nikolić, Aleksandar S.",
year = "2020",
abstract = "A simple organic-phase synthesis process was used to produce bare NiFe2O4 and ZnFe2O4 and core-shell ZnFe2O4@NiFe2O4 ferrite nanoparticles. X-ray powder diffractograms for all investigated powders show characteristic peaks of a spinel cubic structure without a secondary phase. Transmission electron microscopy (TEM) indicated the presence of nanoparticles that are smaller than 20 nm. The release of divalent ions (Ni2+ and Zn2+) from synthesized nanoparticles that were dispersed in saline solution, phosphate-buffered saline (PBS) and human serum, as determined by the inductively coupled plasma mass spectrometry (ICP-MS) method, was lower than 2 wt %. These results demonstrate the stability of the investigated nanoparticles in biologically relevant media and exclude the toxicity of Ni2+ and Zn2+ due to metal ion release, thereby opening a broad range of (bio)medical applications.",
publisher = "Elsevier",
journal = "Ceramics International",
title = "Synthesis, characterization and in vitro evaluation of divalent ion release from stable NiFe2O4, ZnFe2O4 and core-shell ZnFe2O4@NiFe2O4 nanoparticles",
volume = "46",
number = "3",
pages = "3528-3533",
doi = "10.1016/j.ceramint.2019.10.068"
}

Anđelković, L., Jeremić, D., Milenković, M. R., Radosavljević, J., Vulić, P., Pavlović, V. B., Manojlović, D.,& Nikolić, A. S.. (2020). Synthesis, characterization and in vitro evaluation of divalent ion release from stable NiFe2O4, ZnFe2O4 and core-shell ZnFe2O4@NiFe2O4 nanoparticles. in Ceramics International
Elsevier., 46(3), 3528-3533.
https://doi.org/10.1016/j.ceramint.2019.10.068

Anđelković L, Jeremić D, Milenković MR, Radosavljević J, Vulić P, Pavlović VB, Manojlović D, Nikolić AS. Synthesis, characterization and in vitro evaluation of divalent ion release from stable NiFe2O4, ZnFe2O4 and core-shell ZnFe2O4@NiFe2O4 nanoparticles. in Ceramics International. 2020;46(3):3528-3533.
doi:10.1016/j.ceramint.2019.10.068 .

Anđelković, Ljubica, Jeremić, Dejan, Milenković, Milica R., Radosavljević, Jelena, Vulić, Predrag, Pavlović, Vladimir B., Manojlović, Dragan, Nikolić, Aleksandar S., "Synthesis, characterization and in vitro evaluation of divalent ion release from stable NiFe2O4, ZnFe2O4 and core-shell ZnFe2O4@NiFe2O4 nanoparticles" in Ceramics International, 46, no. 3 (2020):3528-3533,
https://doi.org/10.1016/j.ceramint.2019.10.068 . .

TY  - JOUR
AU  - Prodić, I.
AU  - Stanić-Vučinić, Dragana
AU  - Apostolovic, D.
AU  - Mihailović, Jelena
AU  - Radibratović, Milica
AU  - Radosavljevic, J.
AU  - Burazer, L.
AU  - Milčić, Miloš
AU  - Smiljanic, K.
AU  - van, Hage M.
AU  - Ćirković Veličković, Tanja
PY  - 2018
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/2299
AB  - BackgroundMost food allergens sensitizing via the gastrointestinal tract are stable proteins that are resistant to pepsin digestion, in particular major peanut allergens, Ara h 2 and Ara h 6. Survival of their large fragments is essential for sensitizing capacity. However, the immunoreactive proteins/peptides to which the immune system of the gastrointestinal tract is exposed during digestion of peanut proteins are unknown. Particularly, the IgE reactivity of short digestion-resistant peptides (SDRPs;  LT 10kDa) released by gastric digestion under standardized and physiologically relevant invitro conditions has not been investigated. ObjectiveThe aim of this study was to investigate and identify digestion products of major peanut allergens and in particular to examine IgE reactivity of SDRPs released by pepsin digestion of whole peanut grains. MethodsTwo-dimensional gel-based proteomics and shotgun peptidomics, immunoblotting with allergen-specific antibodies from peanut-sensitized patients, enzyme-linked immunosorbent inhibition assay and ImmunoCAP tests, including far ultraviolet-circular dichroism spectroscopy were used to identify and characterize peanut digesta. ResultsAra h 2 and Ara h 6 remained mostly intact, and SDRPs from Ara h 2 were more potent in inhibiting IgE binding than Ara h 1 and Ara 3. Ara h 1 and Ara h 3 exhibited sequential digestion into a series of digestion-resistant peptides with preserved allergenic capacity. A high number of identified SDRPs from Ara h 1, Ara h 2 and Ara h 3 were part of short continuous epitope sequences and possessed substantial allergenic potential. Conclusion and Clinical RelevancePeanut grain digestion by oral and gastric phase enzymes generates mixture of products, where the major peanut allergens remain intact and their digested peptides have preserved allergenic capacity highlighting their important roles in allergic reactions to peanut.
PB  - Wiley, Hoboken
T2  - Clinical and Experimental Allergy
T1  - Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides
VL  - 48
IS  - 6
SP  - 731
EP  - 740
DO  - 10.1111/cea.13113
ER  - 

@article{
author = "Prodić, I. and Stanić-Vučinić, Dragana and Apostolovic, D. and Mihailović, Jelena and Radibratović, Milica and Radosavljevic, J. and Burazer, L. and Milčić, Miloš and Smiljanic, K. and van, Hage M. and Ćirković Veličković, Tanja",
year = "2018",
abstract = "BackgroundMost food allergens sensitizing via the gastrointestinal tract are stable proteins that are resistant to pepsin digestion, in particular major peanut allergens, Ara h 2 and Ara h 6. Survival of their large fragments is essential for sensitizing capacity. However, the immunoreactive proteins/peptides to which the immune system of the gastrointestinal tract is exposed during digestion of peanut proteins are unknown. Particularly, the IgE reactivity of short digestion-resistant peptides (SDRPs;  LT 10kDa) released by gastric digestion under standardized and physiologically relevant invitro conditions has not been investigated. ObjectiveThe aim of this study was to investigate and identify digestion products of major peanut allergens and in particular to examine IgE reactivity of SDRPs released by pepsin digestion of whole peanut grains. MethodsTwo-dimensional gel-based proteomics and shotgun peptidomics, immunoblotting with allergen-specific antibodies from peanut-sensitized patients, enzyme-linked immunosorbent inhibition assay and ImmunoCAP tests, including far ultraviolet-circular dichroism spectroscopy were used to identify and characterize peanut digesta. ResultsAra h 2 and Ara h 6 remained mostly intact, and SDRPs from Ara h 2 were more potent in inhibiting IgE binding than Ara h 1 and Ara 3. Ara h 1 and Ara h 3 exhibited sequential digestion into a series of digestion-resistant peptides with preserved allergenic capacity. A high number of identified SDRPs from Ara h 1, Ara h 2 and Ara h 3 were part of short continuous epitope sequences and possessed substantial allergenic potential. Conclusion and Clinical RelevancePeanut grain digestion by oral and gastric phase enzymes generates mixture of products, where the major peanut allergens remain intact and their digested peptides have preserved allergenic capacity highlighting their important roles in allergic reactions to peanut.",
publisher = "Wiley, Hoboken",
journal = "Clinical and Experimental Allergy",
title = "Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides",
volume = "48",
number = "6",
pages = "731-740",
doi = "10.1111/cea.13113"
}

Prodić, I., Stanić-Vučinić, D., Apostolovic, D., Mihailović, J., Radibratović, M., Radosavljevic, J., Burazer, L., Milčić, M., Smiljanic, K., van, H. M.,& Ćirković Veličković, T.. (2018). Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides. in Clinical and Experimental Allergy
Wiley, Hoboken., 48(6), 731-740.
https://doi.org/10.1111/cea.13113

Prodić I, Stanić-Vučinić D, Apostolovic D, Mihailović J, Radibratović M, Radosavljevic J, Burazer L, Milčić M, Smiljanic K, van HM, Ćirković Veličković T. Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides. in Clinical and Experimental Allergy. 2018;48(6):731-740.
doi:10.1111/cea.13113 .

Prodić, I., Stanić-Vučinić, Dragana, Apostolovic, D., Mihailović, Jelena, Radibratović, Milica, Radosavljevic, J., Burazer, L., Milčić, Miloš, Smiljanic, K., van, Hage M., Ćirković Veličković, Tanja, "Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides" in Clinical and Experimental Allergy, 48, no. 6 (2018):731-740,
https://doi.org/10.1111/cea.13113 . .

TY  - JOUR
AU  - Prodić, I.
AU  - Stanić-Vučinić, Dragana
AU  - Apostolovic, D.
AU  - Mihailović, Jelena
AU  - Radibratović, Milica
AU  - Radosavljevic, J.
AU  - Burazer, L.
AU  - Milčić, Miloš
AU  - Smiljanic, K.
AU  - van, Hage M.
AU  - Ćirković Veličković, Tanja
PY  - 2018
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/3340
AB  - BackgroundMost food allergens sensitizing via the gastrointestinal tract are stable proteins that are resistant to pepsin digestion, in particular major peanut allergens, Ara h 2 and Ara h 6. Survival of their large fragments is essential for sensitizing capacity. However, the immunoreactive proteins/peptides to which the immune system of the gastrointestinal tract is exposed during digestion of peanut proteins are unknown. Particularly, the IgE reactivity of short digestion-resistant peptides (SDRPs;  LT 10kDa) released by gastric digestion under standardized and physiologically relevant invitro conditions has not been investigated. ObjectiveThe aim of this study was to investigate and identify digestion products of major peanut allergens and in particular to examine IgE reactivity of SDRPs released by pepsin digestion of whole peanut grains. MethodsTwo-dimensional gel-based proteomics and shotgun peptidomics, immunoblotting with allergen-specific antibodies from peanut-sensitized patients, enzyme-linked immunosorbent inhibition assay and ImmunoCAP tests, including far ultraviolet-circular dichroism spectroscopy were used to identify and characterize peanut digesta. ResultsAra h 2 and Ara h 6 remained mostly intact, and SDRPs from Ara h 2 were more potent in inhibiting IgE binding than Ara h 1 and Ara 3. Ara h 1 and Ara h 3 exhibited sequential digestion into a series of digestion-resistant peptides with preserved allergenic capacity. A high number of identified SDRPs from Ara h 1, Ara h 2 and Ara h 3 were part of short continuous epitope sequences and possessed substantial allergenic potential. Conclusion and Clinical RelevancePeanut grain digestion by oral and gastric phase enzymes generates mixture of products, where the major peanut allergens remain intact and their digested peptides have preserved allergenic capacity highlighting their important roles in allergic reactions to peanut.
PB  - Wiley, Hoboken
T2  - Clinical and Experimental Allergy
T1  - Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides
VL  - 48
IS  - 6
SP  - 731
EP  - 740
DO  - 10.1111/cea.13113
ER  - 

@article{
author = "Prodić, I. and Stanić-Vučinić, Dragana and Apostolovic, D. and Mihailović, Jelena and Radibratović, Milica and Radosavljevic, J. and Burazer, L. and Milčić, Miloš and Smiljanic, K. and van, Hage M. and Ćirković Veličković, Tanja",
year = "2018",
abstract = "BackgroundMost food allergens sensitizing via the gastrointestinal tract are stable proteins that are resistant to pepsin digestion, in particular major peanut allergens, Ara h 2 and Ara h 6. Survival of their large fragments is essential for sensitizing capacity. However, the immunoreactive proteins/peptides to which the immune system of the gastrointestinal tract is exposed during digestion of peanut proteins are unknown. Particularly, the IgE reactivity of short digestion-resistant peptides (SDRPs;  LT 10kDa) released by gastric digestion under standardized and physiologically relevant invitro conditions has not been investigated. ObjectiveThe aim of this study was to investigate and identify digestion products of major peanut allergens and in particular to examine IgE reactivity of SDRPs released by pepsin digestion of whole peanut grains. MethodsTwo-dimensional gel-based proteomics and shotgun peptidomics, immunoblotting with allergen-specific antibodies from peanut-sensitized patients, enzyme-linked immunosorbent inhibition assay and ImmunoCAP tests, including far ultraviolet-circular dichroism spectroscopy were used to identify and characterize peanut digesta. ResultsAra h 2 and Ara h 6 remained mostly intact, and SDRPs from Ara h 2 were more potent in inhibiting IgE binding than Ara h 1 and Ara 3. Ara h 1 and Ara h 3 exhibited sequential digestion into a series of digestion-resistant peptides with preserved allergenic capacity. A high number of identified SDRPs from Ara h 1, Ara h 2 and Ara h 3 were part of short continuous epitope sequences and possessed substantial allergenic potential. Conclusion and Clinical RelevancePeanut grain digestion by oral and gastric phase enzymes generates mixture of products, where the major peanut allergens remain intact and their digested peptides have preserved allergenic capacity highlighting their important roles in allergic reactions to peanut.",
publisher = "Wiley, Hoboken",
journal = "Clinical and Experimental Allergy",
title = "Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides",
volume = "48",
number = "6",
pages = "731-740",
doi = "10.1111/cea.13113"
}

Prodić, I., Stanić-Vučinić, D., Apostolovic, D., Mihailović, J., Radibratović, M., Radosavljevic, J., Burazer, L., Milčić, M., Smiljanic, K., van, H. M.,& Ćirković Veličković, T.. (2018). Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides. in Clinical and Experimental Allergy
Wiley, Hoboken., 48(6), 731-740.
https://doi.org/10.1111/cea.13113

Prodić I, Stanić-Vučinić D, Apostolovic D, Mihailović J, Radibratović M, Radosavljevic J, Burazer L, Milčić M, Smiljanic K, van HM, Ćirković Veličković T. Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides. in Clinical and Experimental Allergy. 2018;48(6):731-740.
doi:10.1111/cea.13113 .

Prodić, I., Stanić-Vučinić, Dragana, Apostolovic, D., Mihailović, Jelena, Radibratović, Milica, Radosavljevic, J., Burazer, L., Milčić, Miloš, Smiljanic, K., van, Hage M., Ćirković Veličković, Tanja, "Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides" in Clinical and Experimental Allergy, 48, no. 6 (2018):731-740,
https://doi.org/10.1111/cea.13113 . .

TY  - JOUR
AU  - Apostolovic, Danijela
AU  - Stanić-Vučinić, Dragana
AU  - de, Jongh Harmen H J
AU  - de, Jong Govardus A H
AU  - Mihailović, Jelena
AU  - Radosavljević, Jelena
AU  - Radibratović, Milica
AU  - Nordlee, Julie A
AU  - Baumert, Joseph L
AU  - Milčić, Miloš
AU  - Taylor, Steve L
AU  - Clua, Nuria Garrido
AU  - Ćirković Veličković, Tanja
AU  - Koppelman, Stef J
PY  - 2016
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/1853
AB  - Conglutins represent the major peanut allergens and are renowned for their resistance to gastrointestinal digestion. Our aim was to characterize the digestion-resistant peptides (DRPs) of conglutins by biochemical and biophysical methods followed by a molecular dynamics simulation in order to better understand the molecular basis of food protein allergenicity. We have mapped proteolysis sites at the N- and C-termini and at a limited internal segment, while other potential proteolysis sites remained unaffected. Molecular dynamics simulation showed that proteolysis only occurred in the vibrant regions of the proteins. DRPs appeared to be conformationally stable as intact conglutins. Also, the overall secondary structure and IgE-binding potency of DRPs was comparable to that of intact conglutins. The stability of conglutins toward gastro-intestinal digestion, combined with the conformational stability of the resulting DRPs provide conditions for optimal exposure to the intestinal immune system, providing an explanation for the extraordinary allergenicity of peanut conglutins.
PB  - Nature Publishing Group, London
T2  - Scientific Reports
T1  - Conformational stability of digestion-resistant peptides of peanut conglutins reveals the molecular basis of their allergenicity
VL  - 6
DO  - 10.1038/srep29249
ER  - 

@article{
author = "Apostolovic, Danijela and Stanić-Vučinić, Dragana and de, Jongh Harmen H J and de, Jong Govardus A H and Mihailović, Jelena and Radosavljević, Jelena and Radibratović, Milica and Nordlee, Julie A and Baumert, Joseph L and Milčić, Miloš and Taylor, Steve L and Clua, Nuria Garrido and Ćirković Veličković, Tanja and Koppelman, Stef J",
year = "2016",
abstract = "Conglutins represent the major peanut allergens and are renowned for their resistance to gastrointestinal digestion. Our aim was to characterize the digestion-resistant peptides (DRPs) of conglutins by biochemical and biophysical methods followed by a molecular dynamics simulation in order to better understand the molecular basis of food protein allergenicity. We have mapped proteolysis sites at the N- and C-termini and at a limited internal segment, while other potential proteolysis sites remained unaffected. Molecular dynamics simulation showed that proteolysis only occurred in the vibrant regions of the proteins. DRPs appeared to be conformationally stable as intact conglutins. Also, the overall secondary structure and IgE-binding potency of DRPs was comparable to that of intact conglutins. The stability of conglutins toward gastro-intestinal digestion, combined with the conformational stability of the resulting DRPs provide conditions for optimal exposure to the intestinal immune system, providing an explanation for the extraordinary allergenicity of peanut conglutins.",
publisher = "Nature Publishing Group, London",
journal = "Scientific Reports",
title = "Conformational stability of digestion-resistant peptides of peanut conglutins reveals the molecular basis of their allergenicity",
volume = "6",
doi = "10.1038/srep29249"
}

Apostolovic, D., Stanić-Vučinić, D., de, J. H. H. J., de, J. G. A. H., Mihailović, J., Radosavljević, J., Radibratović, M., Nordlee, J. A., Baumert, J. L., Milčić, M., Taylor, S. L., Clua, N. G., Ćirković Veličković, T.,& Koppelman, S. J.. (2016). Conformational stability of digestion-resistant peptides of peanut conglutins reveals the molecular basis of their allergenicity. in Scientific Reports
Nature Publishing Group, London., 6.
https://doi.org/10.1038/srep29249

Apostolovic D, Stanić-Vučinić D, de JHHJ, de JGAH, Mihailović J, Radosavljević J, Radibratović M, Nordlee JA, Baumert JL, Milčić M, Taylor SL, Clua NG, Ćirković Veličković T, Koppelman SJ. Conformational stability of digestion-resistant peptides of peanut conglutins reveals the molecular basis of their allergenicity. in Scientific Reports. 2016;6.
doi:10.1038/srep29249 .

Apostolovic, Danijela, Stanić-Vučinić, Dragana, de, Jongh Harmen H J, de, Jong Govardus A H, Mihailović, Jelena, Radosavljević, Jelena, Radibratović, Milica, Nordlee, Julie A, Baumert, Joseph L, Milčić, Miloš, Taylor, Steve L, Clua, Nuria Garrido, Ćirković Veličković, Tanja, Koppelman, Stef J, "Conformational stability of digestion-resistant peptides of peanut conglutins reveals the molecular basis of their allergenicity" in Scientific Reports, 6 (2016),
https://doi.org/10.1038/srep29249 . .

TY  - JOUR
AU  - Radosavljević, Jelena
AU  - Dobrijevic, Dragana
AU  - Jadranin, Milka
AU  - Blanusa, Milan
AU  - Vukmirica, Jelena
AU  - Ćirković Veličković, Tanja
PY  - 2010
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/709
AB  - BACKGROUND: The major peanut allergens are Ara h 1, Ara h 2 and Ara h 6. Proteolytic processing has been shown to be required for the maturation process of Ara h 6. The aim of this study was to examine whether Ara h 2 undergoes proteolytic processing and, if so, whether proteolytic processing influences its ability to bind human immunoglobulin E (IgE). RESULTS: Ara h 2 isolated from peanut extract under conditions of protease inhibition revealed a single additional peak for its two known isoforms (Ara h 2.01 and Ara h 2.02), corresponding to a C-terminally truncated form lacking a dipeptide (RY). Ara h 2 isolated in the absence of protease inhibition, however, yielded two additional peaks, identified as C-terminally truncated forms lacking either a dipeptide (RY) or a single tyrosine residue. The IgE-binding capacity of the Ara h 2 truncated forms was not altered. CONCLUSION: Ara h 2 undergoes proteolytic processing by peanut proteases that involves C-terminal removal of a dipeptide. Hence Ara h 2 isolated from peanut extract is a complex mixture of two isoforms expressed by different genes, Ara h 2.01 and Ara h 2.02, as well as truncated forms generated by the proteolytic processing of these isoforms.
PB  - John Wiley & Sons Ltd, Chichester
T2  - Journal of the Science of Food and Agriculture
T1  - Insights into proteolytic processing of the major peanut allergen Ara h 2 by endogenous peanut proteases
VL  - 90
IS  - 10
SP  - 1702
EP  - 1708
DO  - 10.1002/jsfa.4005
ER  - 

@article{
author = "Radosavljević, Jelena and Dobrijevic, Dragana and Jadranin, Milka and Blanusa, Milan and Vukmirica, Jelena and Ćirković Veličković, Tanja",
year = "2010",
abstract = "BACKGROUND: The major peanut allergens are Ara h 1, Ara h 2 and Ara h 6. Proteolytic processing has been shown to be required for the maturation process of Ara h 6. The aim of this study was to examine whether Ara h 2 undergoes proteolytic processing and, if so, whether proteolytic processing influences its ability to bind human immunoglobulin E (IgE). RESULTS: Ara h 2 isolated from peanut extract under conditions of protease inhibition revealed a single additional peak for its two known isoforms (Ara h 2.01 and Ara h 2.02), corresponding to a C-terminally truncated form lacking a dipeptide (RY). Ara h 2 isolated in the absence of protease inhibition, however, yielded two additional peaks, identified as C-terminally truncated forms lacking either a dipeptide (RY) or a single tyrosine residue. The IgE-binding capacity of the Ara h 2 truncated forms was not altered. CONCLUSION: Ara h 2 undergoes proteolytic processing by peanut proteases that involves C-terminal removal of a dipeptide. Hence Ara h 2 isolated from peanut extract is a complex mixture of two isoforms expressed by different genes, Ara h 2.01 and Ara h 2.02, as well as truncated forms generated by the proteolytic processing of these isoforms.",
publisher = "John Wiley & Sons Ltd, Chichester",
journal = "Journal of the Science of Food and Agriculture",
title = "Insights into proteolytic processing of the major peanut allergen Ara h 2 by endogenous peanut proteases",
volume = "90",
number = "10",
pages = "1702-1708",
doi = "10.1002/jsfa.4005"
}

Radosavljević, J., Dobrijevic, D., Jadranin, M., Blanusa, M., Vukmirica, J.,& Ćirković Veličković, T.. (2010). Insights into proteolytic processing of the major peanut allergen Ara h 2 by endogenous peanut proteases. in Journal of the Science of Food and Agriculture
John Wiley & Sons Ltd, Chichester., 90(10), 1702-1708.
https://doi.org/10.1002/jsfa.4005

Radosavljević J, Dobrijevic D, Jadranin M, Blanusa M, Vukmirica J, Ćirković Veličković T. Insights into proteolytic processing of the major peanut allergen Ara h 2 by endogenous peanut proteases. in Journal of the Science of Food and Agriculture. 2010;90(10):1702-1708.
doi:10.1002/jsfa.4005 .

Radosavljević, Jelena, Dobrijevic, Dragana, Jadranin, Milka, Blanusa, Milan, Vukmirica, Jelena, Ćirković Veličković, Tanja, "Insights into proteolytic processing of the major peanut allergen Ara h 2 by endogenous peanut proteases" in Journal of the Science of Food and Agriculture, 90, no. 10 (2010):1702-1708,
https://doi.org/10.1002/jsfa.4005 . .

TY  - JOUR
AU  - Stanić, Dragana
AU  - Monogioudi, Evanthia
AU  - Dilek, Ercili
AU  - Radosavljević, Jelena
AU  - Atanasković-Marković, Marina
AU  - Vuckovic, Olga
AU  - Raija, Lantto
AU  - Mattinen, Maija
AU  - Buchert, Johanna
AU  - Ćirković-Veličković, Tanja
PY  - 2010
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/4168
AB  - Crosslinking enzymes are frequently used in bioprocessing of dairy products. The aim of this study was to examine the effects of enzymatic crosslinking on IgE binding, allergenicity and digestion stability of beta-casein (CN). beta-CN was crosslinked by transglutaminase, tyrosinase, mushroom tyrosinase/caffeic acid and laccase/caffeic acid. The IgE binding to beta-CN was compared in vitro by CAP inhibition assay, ELISA inhibition as well as ex vivo by basophil activation assay. Crosslinked CNs were digested by simulated gastric fluid for 15 and 60 min and obtained digests analyzed for their ability to inhibit IgE binding by CAP inhibition assay and SDS-PAGE. The ability of crosslinked CNs to activate basophils was significantly reduced in seven patients in the case of CN crosslinked by laccase and moderately reduced in the case of tyrosinase/caffeic acid crosslinked CN (in two cow's milk allergy patients tested with different allergen concentrations). The response to various crosslinked CNs differed individually among patients' sera tested by ELISA inhibition assay. The presence of caffeic acid hampered digestion by pepsin, and this effect was most pronounced for the tyrosinase/caffeic acid crosslinked CN. The laccase/caffeic acid and mushroom tyrosinase/caffeic acid had the highest potential in mitigating IgE binding and allergenicity of the beta-CN out of all investigated enzymes. The presence of a small phenolic compound also increased digestion stability of beta-CN.
PB  - Wiley
T2  - Molecular Nutrition and Food Research
T1  - Digestibility and allergenicity assessment of enzymatically crosslinked beta-casein
VL  - 54
IS  - 9
SP  - 1273
EP  - 1284
DO  - 10.1002/mnfr.200900184
ER  - 

@article{
author = "Stanić, Dragana and Monogioudi, Evanthia and Dilek, Ercili and Radosavljević, Jelena and Atanasković-Marković, Marina and Vuckovic, Olga and Raija, Lantto and Mattinen, Maija and Buchert, Johanna and Ćirković-Veličković, Tanja",
year = "2010",
abstract = "Crosslinking enzymes are frequently used in bioprocessing of dairy products. The aim of this study was to examine the effects of enzymatic crosslinking on IgE binding, allergenicity and digestion stability of beta-casein (CN). beta-CN was crosslinked by transglutaminase, tyrosinase, mushroom tyrosinase/caffeic acid and laccase/caffeic acid. The IgE binding to beta-CN was compared in vitro by CAP inhibition assay, ELISA inhibition as well as ex vivo by basophil activation assay. Crosslinked CNs were digested by simulated gastric fluid for 15 and 60 min and obtained digests analyzed for their ability to inhibit IgE binding by CAP inhibition assay and SDS-PAGE. The ability of crosslinked CNs to activate basophils was significantly reduced in seven patients in the case of CN crosslinked by laccase and moderately reduced in the case of tyrosinase/caffeic acid crosslinked CN (in two cow's milk allergy patients tested with different allergen concentrations). The response to various crosslinked CNs differed individually among patients' sera tested by ELISA inhibition assay. The presence of caffeic acid hampered digestion by pepsin, and this effect was most pronounced for the tyrosinase/caffeic acid crosslinked CN. The laccase/caffeic acid and mushroom tyrosinase/caffeic acid had the highest potential in mitigating IgE binding and allergenicity of the beta-CN out of all investigated enzymes. The presence of a small phenolic compound also increased digestion stability of beta-CN.",
publisher = "Wiley",
journal = "Molecular Nutrition and Food Research",
title = "Digestibility and allergenicity assessment of enzymatically crosslinked beta-casein",
volume = "54",
number = "9",
pages = "1273-1284",
doi = "10.1002/mnfr.200900184"
}

Stanić, D., Monogioudi, E., Dilek, E., Radosavljević, J., Atanasković-Marković, M., Vuckovic, O., Raija, L., Mattinen, M., Buchert, J.,& Ćirković-Veličković, T.. (2010). Digestibility and allergenicity assessment of enzymatically crosslinked beta-casein. in Molecular Nutrition and Food Research
Wiley., 54(9), 1273-1284.
https://doi.org/10.1002/mnfr.200900184

Stanić D, Monogioudi E, Dilek E, Radosavljević J, Atanasković-Marković M, Vuckovic O, Raija L, Mattinen M, Buchert J, Ćirković-Veličković T. Digestibility and allergenicity assessment of enzymatically crosslinked beta-casein. in Molecular Nutrition and Food Research. 2010;54(9):1273-1284.
doi:10.1002/mnfr.200900184 .

Stanić, Dragana, Monogioudi, Evanthia, Dilek, Ercili, Radosavljević, Jelena, Atanasković-Marković, Marina, Vuckovic, Olga, Raija, Lantto, Mattinen, Maija, Buchert, Johanna, Ćirković-Veličković, Tanja, "Digestibility and allergenicity assessment of enzymatically crosslinked beta-casein" in Molecular Nutrition and Food Research, 54, no. 9 (2010):1273-1284,
https://doi.org/10.1002/mnfr.200900184 . .