TY  - DATA
AU  - Mihajlović, L.
AU  - Radosavljević, Jelena
AU  - Nordlund, Emilia
AU  - Krstić-Ristivojević, Maja
AU  - Bohn, Torsten
AU  - Smit, Joost
AU  - Buchert, Johanna
AU  - Ćirković-Veličković, Tanja
PY  - 2016
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3591
PB  - Royal Soc Chemistry, Cambridge
T2  - Food and Function
T1  - Supplementary data for the article: Mihajlovic, L.; Radosavljevic, J.; Nordlund, E.; Krstic, M.; Bohn, T.; Smit, J.; Buchert, J.; Cirkovic Velickovic, T. Peanut Protein Structure, Polyphenol Content and Immune Response to Peanut Proteins: In Vivo Are Modulated by Laccase. Food and Function 2016, 7 (5), 2357–2366. https://doi.org/10.1039/c5fo01325a
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3591
ER  - 

@misc{
author = "Mihajlović, L. and Radosavljević, Jelena and Nordlund, Emilia and Krstić-Ristivojević, Maja and Bohn, Torsten and Smit, Joost and Buchert, Johanna and Ćirković-Veličković, Tanja",
year = "2016",
publisher = "Royal Soc Chemistry, Cambridge",
journal = "Food and Function",
title = "Supplementary data for the article: Mihajlovic, L.; Radosavljevic, J.; Nordlund, E.; Krstic, M.; Bohn, T.; Smit, J.; Buchert, J.; Cirkovic Velickovic, T. Peanut Protein Structure, Polyphenol Content and Immune Response to Peanut Proteins: In Vivo Are Modulated by Laccase. Food and Function 2016, 7 (5), 2357–2366. https://doi.org/10.1039/c5fo01325a",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3591"
}

Mihajlović, L., Radosavljević, J., Nordlund, E., Krstić-Ristivojević, M., Bohn, T., Smit, J., Buchert, J.,& Ćirković-Veličković, T.. (2016). Supplementary data for the article: Mihajlovic, L.; Radosavljevic, J.; Nordlund, E.; Krstic, M.; Bohn, T.; Smit, J.; Buchert, J.; Cirkovic Velickovic, T. Peanut Protein Structure, Polyphenol Content and Immune Response to Peanut Proteins: In Vivo Are Modulated by Laccase. Food and Function 2016, 7 (5), 2357–2366. https://doi.org/10.1039/c5fo01325a. in Food and Function
Royal Soc Chemistry, Cambridge..
https://hdl.handle.net/21.15107/rcub_cherry_3591

Mihajlović L, Radosavljević J, Nordlund E, Krstić-Ristivojević M, Bohn T, Smit J, Buchert J, Ćirković-Veličković T. Supplementary data for the article: Mihajlovic, L.; Radosavljevic, J.; Nordlund, E.; Krstic, M.; Bohn, T.; Smit, J.; Buchert, J.; Cirkovic Velickovic, T. Peanut Protein Structure, Polyphenol Content and Immune Response to Peanut Proteins: In Vivo Are Modulated by Laccase. Food and Function 2016, 7 (5), 2357–2366. https://doi.org/10.1039/c5fo01325a. in Food and Function. 2016;.
https://hdl.handle.net/21.15107/rcub_cherry_3591 .

Mihajlović, L., Radosavljević, Jelena, Nordlund, Emilia, Krstić-Ristivojević, Maja, Bohn, Torsten, Smit, Joost, Buchert, Johanna, Ćirković-Veličković, Tanja, "Supplementary data for the article: Mihajlovic, L.; Radosavljevic, J.; Nordlund, E.; Krstic, M.; Bohn, T.; Smit, J.; Buchert, J.; Cirkovic Velickovic, T. Peanut Protein Structure, Polyphenol Content and Immune Response to Peanut Proteins: In Vivo Are Modulated by Laccase. Food and Function 2016, 7 (5), 2357–2366. https://doi.org/10.1039/c5fo01325a" in Food and Function (2016),
https://hdl.handle.net/21.15107/rcub_cherry_3591 .

TY  - JOUR
AU  - Mihajlović, L.
AU  - Radosavljević, Jelena
AU  - Nordlund, Emilia
AU  - Krstić-Ristivojević, Maja
AU  - Bohn, Torsten
AU  - Smit, Joost
AU  - Buchert, Johanna
AU  - Ćirković-Veličković, Tanja
PY  - 2016
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2254
AB  - Food texture can be improved by enzyme-mediated covalent cross-linking of different food components, such as proteins and carbohydrates. Cross-linking changes the biological and immunological properties of proteins and may change the sensitizing potential of food allergens. In this study we applied a microbial polyphenol oxidase, laccase, to cross-link peanut proteins. The size and morphology of the obtained cross-linked proteins were analyzed by electrophoresis and electron microscopy. Structural changes in proteins were analyzed by CD spectroscopy and by using specific antibodies to major peanut allergens. The bioavailability of peanut proteins was analyzed using a Caco-2 epithelial cell model. The in vivo sensitizing potential of laccase-treated peanut proteins was analyzed using a mouse model of food allergy. Finally, peanut polyphenols were analyzed by UHPLC-MS/MS, before and after the enzymatic reaction with laccase. Laccase treatment of peanut proteins yielded a covalently cross-linked material, with the modified tertiary structure of peanut proteins, improved bioavailability of Ara h 2 (by 70 fold, p  lt  0.05) and modulated allergic immune response in vivo. The modulation of the immune response was related to the increased production of IgG2a antibodies 11 fold (p  lt  0.05) and reduced IL-13 secretion in in vitro cultured splenocytes 7 fold (p  lt  0.05). Analysis of the peanut polyphenol content and profile by HPLC-MS/MS revealed that laccase treatment depleted the peanut extract of polyphenol compounds leaving mostly isorhamnetin derivatives and procyanidin dimer B-type in detectable amounts. Treatment of complex food extracts rich in polyphenols with laccase results in both protein cross-linking and modification of polyphenol compounds. These extensively cross-linked proteins have unchanged potency to induce allergic sensitization in vivo, but certain immunomodulatory changes were observed.
PB  - Royal Soc Chemistry, Cambridge
T2  - Food and Function
T1  - Peanut protein structure, polyphenol content and immune response to peanut proteins in vivo are modulated by laccase
VL  - 7
IS  - 5
SP  - 2357
EP  - 2366
DO  - 10.1039/c5fo01325a
ER  - 

@article{
author = "Mihajlović, L. and Radosavljević, Jelena and Nordlund, Emilia and Krstić-Ristivojević, Maja and Bohn, Torsten and Smit, Joost and Buchert, Johanna and Ćirković-Veličković, Tanja",
year = "2016",
abstract = "Food texture can be improved by enzyme-mediated covalent cross-linking of different food components, such as proteins and carbohydrates. Cross-linking changes the biological and immunological properties of proteins and may change the sensitizing potential of food allergens. In this study we applied a microbial polyphenol oxidase, laccase, to cross-link peanut proteins. The size and morphology of the obtained cross-linked proteins were analyzed by electrophoresis and electron microscopy. Structural changes in proteins were analyzed by CD spectroscopy and by using specific antibodies to major peanut allergens. The bioavailability of peanut proteins was analyzed using a Caco-2 epithelial cell model. The in vivo sensitizing potential of laccase-treated peanut proteins was analyzed using a mouse model of food allergy. Finally, peanut polyphenols were analyzed by UHPLC-MS/MS, before and after the enzymatic reaction with laccase. Laccase treatment of peanut proteins yielded a covalently cross-linked material, with the modified tertiary structure of peanut proteins, improved bioavailability of Ara h 2 (by 70 fold, p  lt  0.05) and modulated allergic immune response in vivo. The modulation of the immune response was related to the increased production of IgG2a antibodies 11 fold (p  lt  0.05) and reduced IL-13 secretion in in vitro cultured splenocytes 7 fold (p  lt  0.05). Analysis of the peanut polyphenol content and profile by HPLC-MS/MS revealed that laccase treatment depleted the peanut extract of polyphenol compounds leaving mostly isorhamnetin derivatives and procyanidin dimer B-type in detectable amounts. Treatment of complex food extracts rich in polyphenols with laccase results in both protein cross-linking and modification of polyphenol compounds. These extensively cross-linked proteins have unchanged potency to induce allergic sensitization in vivo, but certain immunomodulatory changes were observed.",
publisher = "Royal Soc Chemistry, Cambridge",
journal = "Food and Function",
title = "Peanut protein structure, polyphenol content and immune response to peanut proteins in vivo are modulated by laccase",
volume = "7",
number = "5",
pages = "2357-2366",
doi = "10.1039/c5fo01325a"
}

Mihajlović, L., Radosavljević, J., Nordlund, E., Krstić-Ristivojević, M., Bohn, T., Smit, J., Buchert, J.,& Ćirković-Veličković, T.. (2016). Peanut protein structure, polyphenol content and immune response to peanut proteins in vivo are modulated by laccase. in Food and Function
Royal Soc Chemistry, Cambridge., 7(5), 2357-2366.
https://doi.org/10.1039/c5fo01325a

Mihajlović L, Radosavljević J, Nordlund E, Krstić-Ristivojević M, Bohn T, Smit J, Buchert J, Ćirković-Veličković T. Peanut protein structure, polyphenol content and immune response to peanut proteins in vivo are modulated by laccase. in Food and Function. 2016;7(5):2357-2366.
doi:10.1039/c5fo01325a .

Mihajlović, L., Radosavljević, Jelena, Nordlund, Emilia, Krstić-Ristivojević, Maja, Bohn, Torsten, Smit, Joost, Buchert, Johanna, Ćirković-Veličković, Tanja, "Peanut protein structure, polyphenol content and immune response to peanut proteins in vivo are modulated by laccase" in Food and Function, 7, no. 5 (2016):2357-2366,
https://doi.org/10.1039/c5fo01325a . .

TY  - JOUR
AU  - Radosavljević, Jelena
AU  - Nordlund, Emilia
AU  - Mihajlovic, Luka
AU  - Krstić-Ristivojević, Maja
AU  - Bohn, Torsten
AU  - Buchert, Johanna
AU  - Ćirković-Veličković, Tanja
AU  - Smit, Joost
PY  - 2014
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1510
AB  - ScopeThe cross-linking of proteins by enzymes to form high-molecular-weight protein, aggregates can be used to tailor the technological or physiological functionality of food products. Aggregation of dietary proteins by food processing may promote allergic sensitization, but the effects of enzymatic cross-linking of dietary proteins on the allergenic potential of food are not known. In this study, the bioavailability and the sensitizing or tolerizing potential of peanut proteins (PE) cross-linked with microbial tyrosinase from Trichoderma reesei and mushroom tyrosinase from Agaricus bisporus, were investigated. Methods and resultsThe impact of cross-linking of PE on the in vitro bioavailability of fluorescein isothiocyanate-labeled peanut proteins was tested in a Caco-2 cell monolayer and by competitive ELISA. The in vivo allergenicity or capacity to induce oral tolerance in mice were measured by serum levels of PE-specific antibodies and T cell cytokine production after exposure to PE and cross-linked PE. ConclusionEnzymatic processing of peanut proteins by the two tyrosinases increased the bioavailability of major peanut allergen Ara h 2, but did not significantly change the allergenic or tolerizing properties of peanut. Enzymatic treatment of peanut proteins yielded cross-linked proteins with preserved molecular and immunological features of peanut allergens.
PB  - Wiley-Blackwell, Hoboken
T2  - Molecular Nutrition and Food Research
T1  - Sensitizing potential of enzymatically cross-linked peanut proteins in a mouse model of peanut allergy
VL  - 58
IS  - 3
SP  - 635
EP  - 646
DO  - 10.1002/mnfr.201300403
ER  - 

@article{
author = "Radosavljević, Jelena and Nordlund, Emilia and Mihajlovic, Luka and Krstić-Ristivojević, Maja and Bohn, Torsten and Buchert, Johanna and Ćirković-Veličković, Tanja and Smit, Joost",
year = "2014",
abstract = "ScopeThe cross-linking of proteins by enzymes to form high-molecular-weight protein, aggregates can be used to tailor the technological or physiological functionality of food products. Aggregation of dietary proteins by food processing may promote allergic sensitization, but the effects of enzymatic cross-linking of dietary proteins on the allergenic potential of food are not known. In this study, the bioavailability and the sensitizing or tolerizing potential of peanut proteins (PE) cross-linked with microbial tyrosinase from Trichoderma reesei and mushroom tyrosinase from Agaricus bisporus, were investigated. Methods and resultsThe impact of cross-linking of PE on the in vitro bioavailability of fluorescein isothiocyanate-labeled peanut proteins was tested in a Caco-2 cell monolayer and by competitive ELISA. The in vivo allergenicity or capacity to induce oral tolerance in mice were measured by serum levels of PE-specific antibodies and T cell cytokine production after exposure to PE and cross-linked PE. ConclusionEnzymatic processing of peanut proteins by the two tyrosinases increased the bioavailability of major peanut allergen Ara h 2, but did not significantly change the allergenic or tolerizing properties of peanut. Enzymatic treatment of peanut proteins yielded cross-linked proteins with preserved molecular and immunological features of peanut allergens.",
publisher = "Wiley-Blackwell, Hoboken",
journal = "Molecular Nutrition and Food Research",
title = "Sensitizing potential of enzymatically cross-linked peanut proteins in a mouse model of peanut allergy",
volume = "58",
number = "3",
pages = "635-646",
doi = "10.1002/mnfr.201300403"
}

Radosavljević, J., Nordlund, E., Mihajlovic, L., Krstić-Ristivojević, M., Bohn, T., Buchert, J., Ćirković-Veličković, T.,& Smit, J.. (2014). Sensitizing potential of enzymatically cross-linked peanut proteins in a mouse model of peanut allergy. in Molecular Nutrition and Food Research
Wiley-Blackwell, Hoboken., 58(3), 635-646.
https://doi.org/10.1002/mnfr.201300403

Radosavljević J, Nordlund E, Mihajlovic L, Krstić-Ristivojević M, Bohn T, Buchert J, Ćirković-Veličković T, Smit J. Sensitizing potential of enzymatically cross-linked peanut proteins in a mouse model of peanut allergy. in Molecular Nutrition and Food Research. 2014;58(3):635-646.
doi:10.1002/mnfr.201300403 .

Radosavljević, Jelena, Nordlund, Emilia, Mihajlovic, Luka, Krstić-Ristivojević, Maja, Bohn, Torsten, Buchert, Johanna, Ćirković-Veličković, Tanja, Smit, Joost, "Sensitizing potential of enzymatically cross-linked peanut proteins in a mouse model of peanut allergy" in Molecular Nutrition and Food Research, 58, no. 3 (2014):635-646,
https://doi.org/10.1002/mnfr.201300403 . .

TY  - JOUR
AU  - Stojadinović, Marija M.
AU  - Burazer, Lidija M.
AU  - Ercili-Cura, Dilek
AU  - Sancho, Ana
AU  - Buchert, Johanna
AU  - Ćirković-Veličković, Tanja
AU  - Stanić-Vučinić, Dragana
PY  - 2012
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1275
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5261
AB  - BACKGROUND: The major whey protein beta-lactoglobulin (BLG) has been widely studied for its functional properties. The aim of this study was to develop an efficient, inexpensive and rapid one-step method for the isolation and purification of BLG while preserving its native structure. RESULTS: BLGwas purified fromdefattedwheyobtainedfromrawcow's milkbyanionexchangechromatography. Protein purity and identitywere determined using reverse phase high-performance liquid chromatography andmass spectrometry. Total BLG yield was 80% with protein purity from 97 to 99%. BLG isoforms A and B were separated into fractions of 91 and 99% purity respectively. The structure and native conformation of the isolated BLGwere compared with those of standard commercial BLG by circular dichroism spectrometry, susceptibility to various crosslinking enzymes and enzyme-linked immunosorbent assay inhibition. CONCLUSION: Theproposedmethodis veryuseful for the rapid preparationofBLGsuitable for studying antigenicandmolecular characteristics of this protein, aswell as the effect of food processing on these properties. The procedure requires only 1 day for the purification of about 300 mgof BLG from a single run using a small column (2.5 cmx20 cm) of diethylaminoethyl Sephadex and has potential for scaling up. (C) 2011 Society of Chemical Industry
PB  - Wiley-Blackwell, Malden
T2  - Journal of the Science of Food and Agriculture
T1  - One-step method for isolation and purification of native beta-lactoglobulin from bovine whey
VL  - 92
IS  - 7
SP  - 1432
EP  - 1440
DO  - 10.1002/jsfa.4722
ER  - 

@article{
author = "Stojadinović, Marija M. and Burazer, Lidija M. and Ercili-Cura, Dilek and Sancho, Ana and Buchert, Johanna and Ćirković-Veličković, Tanja and Stanić-Vučinić, Dragana",
year = "2012",
abstract = "BACKGROUND: The major whey protein beta-lactoglobulin (BLG) has been widely studied for its functional properties. The aim of this study was to develop an efficient, inexpensive and rapid one-step method for the isolation and purification of BLG while preserving its native structure. RESULTS: BLGwas purified fromdefattedwheyobtainedfromrawcow's milkbyanionexchangechromatography. Protein purity and identitywere determined using reverse phase high-performance liquid chromatography andmass spectrometry. Total BLG yield was 80% with protein purity from 97 to 99%. BLG isoforms A and B were separated into fractions of 91 and 99% purity respectively. The structure and native conformation of the isolated BLGwere compared with those of standard commercial BLG by circular dichroism spectrometry, susceptibility to various crosslinking enzymes and enzyme-linked immunosorbent assay inhibition. CONCLUSION: Theproposedmethodis veryuseful for the rapid preparationofBLGsuitable for studying antigenicandmolecular characteristics of this protein, aswell as the effect of food processing on these properties. The procedure requires only 1 day for the purification of about 300 mgof BLG from a single run using a small column (2.5 cmx20 cm) of diethylaminoethyl Sephadex and has potential for scaling up. (C) 2011 Society of Chemical Industry",
publisher = "Wiley-Blackwell, Malden",
journal = "Journal of the Science of Food and Agriculture",
title = "One-step method for isolation and purification of native beta-lactoglobulin from bovine whey",
volume = "92",
number = "7",
pages = "1432-1440",
doi = "10.1002/jsfa.4722"
}

Stojadinović, M. M., Burazer, L. M., Ercili-Cura, D., Sancho, A., Buchert, J., Ćirković-Veličković, T.,& Stanić-Vučinić, D.. (2012). One-step method for isolation and purification of native beta-lactoglobulin from bovine whey. in Journal of the Science of Food and Agriculture
Wiley-Blackwell, Malden., 92(7), 1432-1440.
https://doi.org/10.1002/jsfa.4722

Stojadinović MM, Burazer LM, Ercili-Cura D, Sancho A, Buchert J, Ćirković-Veličković T, Stanić-Vučinić D. One-step method for isolation and purification of native beta-lactoglobulin from bovine whey. in Journal of the Science of Food and Agriculture. 2012;92(7):1432-1440.
doi:10.1002/jsfa.4722 .

Stojadinović, Marija M., Burazer, Lidija M., Ercili-Cura, Dilek, Sancho, Ana, Buchert, Johanna, Ćirković-Veličković, Tanja, Stanić-Vučinić, Dragana, "One-step method for isolation and purification of native beta-lactoglobulin from bovine whey" in Journal of the Science of Food and Agriculture, 92, no. 7 (2012):1432-1440,
https://doi.org/10.1002/jsfa.4722 . .

TY  - JOUR
AU  - Stojadinović, Marija M.
AU  - Burazer, Lidija M.
AU  - Ercili-Cura, Dilek
AU  - Sancho, Ana
AU  - Buchert, Johanna
AU  - Ćirković-Veličković, Tanja
AU  - Stanić-Vučinić, Dragana
PY  - 2012
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1275
AB  - BACKGROUND: The major whey protein beta-lactoglobulin (BLG) has been widely studied for its functional properties. The aim of this study was to develop an efficient, inexpensive and rapid one-step method for the isolation and purification of BLG while preserving its native structure. RESULTS: BLGwas purified fromdefattedwheyobtainedfromrawcow's milkbyanionexchangechromatography. Protein purity and identitywere determined using reverse phase high-performance liquid chromatography andmass spectrometry. Total BLG yield was 80% with protein purity from 97 to 99%. BLG isoforms A and B were separated into fractions of 91 and 99% purity respectively. The structure and native conformation of the isolated BLGwere compared with those of standard commercial BLG by circular dichroism spectrometry, susceptibility to various crosslinking enzymes and enzyme-linked immunosorbent assay inhibition. CONCLUSION: Theproposedmethodis veryuseful for the rapid preparationofBLGsuitable for studying antigenicandmolecular characteristics of this protein, aswell as the effect of food processing on these properties. The procedure requires only 1 day for the purification of about 300 mgof BLG from a single run using a small column (2.5 cmx20 cm) of diethylaminoethyl Sephadex and has potential for scaling up. (C) 2011 Society of Chemical Industry
PB  - Wiley-Blackwell, Malden
T2  - Journal of the Science of Food and Agriculture
T1  - One-step method for isolation and purification of native beta-lactoglobulin from bovine whey
VL  - 92
IS  - 7
SP  - 1432
EP  - 1440
DO  - 10.1002/jsfa.4722
ER  - 

@article{
author = "Stojadinović, Marija M. and Burazer, Lidija M. and Ercili-Cura, Dilek and Sancho, Ana and Buchert, Johanna and Ćirković-Veličković, Tanja and Stanić-Vučinić, Dragana",
year = "2012",
abstract = "BACKGROUND: The major whey protein beta-lactoglobulin (BLG) has been widely studied for its functional properties. The aim of this study was to develop an efficient, inexpensive and rapid one-step method for the isolation and purification of BLG while preserving its native structure. RESULTS: BLGwas purified fromdefattedwheyobtainedfromrawcow's milkbyanionexchangechromatography. Protein purity and identitywere determined using reverse phase high-performance liquid chromatography andmass spectrometry. Total BLG yield was 80% with protein purity from 97 to 99%. BLG isoforms A and B were separated into fractions of 91 and 99% purity respectively. The structure and native conformation of the isolated BLGwere compared with those of standard commercial BLG by circular dichroism spectrometry, susceptibility to various crosslinking enzymes and enzyme-linked immunosorbent assay inhibition. CONCLUSION: Theproposedmethodis veryuseful for the rapid preparationofBLGsuitable for studying antigenicandmolecular characteristics of this protein, aswell as the effect of food processing on these properties. The procedure requires only 1 day for the purification of about 300 mgof BLG from a single run using a small column (2.5 cmx20 cm) of diethylaminoethyl Sephadex and has potential for scaling up. (C) 2011 Society of Chemical Industry",
publisher = "Wiley-Blackwell, Malden",
journal = "Journal of the Science of Food and Agriculture",
title = "One-step method for isolation and purification of native beta-lactoglobulin from bovine whey",
volume = "92",
number = "7",
pages = "1432-1440",
doi = "10.1002/jsfa.4722"
}

Stojadinović, M. M., Burazer, L. M., Ercili-Cura, D., Sancho, A., Buchert, J., Ćirković-Veličković, T.,& Stanić-Vučinić, D.. (2012). One-step method for isolation and purification of native beta-lactoglobulin from bovine whey. in Journal of the Science of Food and Agriculture
Wiley-Blackwell, Malden., 92(7), 1432-1440.
https://doi.org/10.1002/jsfa.4722

Stojadinović MM, Burazer LM, Ercili-Cura D, Sancho A, Buchert J, Ćirković-Veličković T, Stanić-Vučinić D. One-step method for isolation and purification of native beta-lactoglobulin from bovine whey. in Journal of the Science of Food and Agriculture. 2012;92(7):1432-1440.
doi:10.1002/jsfa.4722 .

Stojadinović, Marija M., Burazer, Lidija M., Ercili-Cura, Dilek, Sancho, Ana, Buchert, Johanna, Ćirković-Veličković, Tanja, Stanić-Vučinić, Dragana, "One-step method for isolation and purification of native beta-lactoglobulin from bovine whey" in Journal of the Science of Food and Agriculture, 92, no. 7 (2012):1432-1440,
https://doi.org/10.1002/jsfa.4722 . .

TY  - CONF
AU  - Mihajlović, L.
AU  - Radosavljević, Jelena
AU  - Nordlund, Emilia
AU  - Smit, Joost
AU  - Buchert, Johanna
AU  - Ćirković-Veličković, Tanja
PY  - 2011
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1592
PB  - Wiley-Blackwell, Hoboken
C3  - Allergy
T1  - Optimisation of peanut protein crosslinking by oxidase and transglutaminase enzymes and the effects on IgE binding
VL  - 66
SP  - 536
EP  - 536
UR  - https://hdl.handle.net/21.15107/rcub_cherry_1592
ER  - 

@conference{
author = "Mihajlović, L. and Radosavljević, Jelena and Nordlund, Emilia and Smit, Joost and Buchert, Johanna and Ćirković-Veličković, Tanja",
year = "2011",
publisher = "Wiley-Blackwell, Hoboken",
journal = "Allergy",
title = "Optimisation of peanut protein crosslinking by oxidase and transglutaminase enzymes and the effects on IgE binding",
volume = "66",
pages = "536-536",
url = "https://hdl.handle.net/21.15107/rcub_cherry_1592"
}

Mihajlović, L., Radosavljević, J., Nordlund, E., Smit, J., Buchert, J.,& Ćirković-Veličković, T.. (2011). Optimisation of peanut protein crosslinking by oxidase and transglutaminase enzymes and the effects on IgE binding. in Allergy
Wiley-Blackwell, Hoboken., 66, 536-536.
https://hdl.handle.net/21.15107/rcub_cherry_1592

Mihajlović L, Radosavljević J, Nordlund E, Smit J, Buchert J, Ćirković-Veličković T. Optimisation of peanut protein crosslinking by oxidase and transglutaminase enzymes and the effects on IgE binding. in Allergy. 2011;66:536-536.
https://hdl.handle.net/21.15107/rcub_cherry_1592 .

Mihajlović, L., Radosavljević, Jelena, Nordlund, Emilia, Smit, Joost, Buchert, Johanna, Ćirković-Veličković, Tanja, "Optimisation of peanut protein crosslinking by oxidase and transglutaminase enzymes and the effects on IgE binding" in Allergy, 66 (2011):536-536,
https://hdl.handle.net/21.15107/rcub_cherry_1592 .

TY  - CONF
AU  - Stojadinović, Marija M.
AU  - Burazer, Lidija M.
AU  - Ercili-Cura, D.
AU  - Sancho, A.
AU  - Buchert, Johanna
AU  - Mills, C.
AU  - Ćirković-Veličković, Tanja
AU  - Stanić-Vučinić, Dragana
PY  - 2011
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1473
PB  - Wiley-Blackwell, Hoboken
C3  - Allergy
T1  - An improved method for isolation and purification of native bovine beta-lactoglobulin; separation of A and B beta-lactoglobulin isoforms
VL  - 66
SP  - 523
EP  - 524
UR  - https://hdl.handle.net/21.15107/rcub_cherry_1473
ER  - 

@conference{
author = "Stojadinović, Marija M. and Burazer, Lidija M. and Ercili-Cura, D. and Sancho, A. and Buchert, Johanna and Mills, C. and Ćirković-Veličković, Tanja and Stanić-Vučinić, Dragana",
year = "2011",
publisher = "Wiley-Blackwell, Hoboken",
journal = "Allergy",
title = "An improved method for isolation and purification of native bovine beta-lactoglobulin; separation of A and B beta-lactoglobulin isoforms",
volume = "66",
pages = "523-524",
url = "https://hdl.handle.net/21.15107/rcub_cherry_1473"
}

Stojadinović, M. M., Burazer, L. M., Ercili-Cura, D., Sancho, A., Buchert, J., Mills, C., Ćirković-Veličković, T.,& Stanić-Vučinić, D.. (2011). An improved method for isolation and purification of native bovine beta-lactoglobulin; separation of A and B beta-lactoglobulin isoforms. in Allergy
Wiley-Blackwell, Hoboken., 66, 523-524.
https://hdl.handle.net/21.15107/rcub_cherry_1473

Stojadinović MM, Burazer LM, Ercili-Cura D, Sancho A, Buchert J, Mills C, Ćirković-Veličković T, Stanić-Vučinić D. An improved method for isolation and purification of native bovine beta-lactoglobulin; separation of A and B beta-lactoglobulin isoforms. in Allergy. 2011;66:523-524.
https://hdl.handle.net/21.15107/rcub_cherry_1473 .

Stojadinović, Marija M., Burazer, Lidija M., Ercili-Cura, D., Sancho, A., Buchert, Johanna, Mills, C., Ćirković-Veličković, Tanja, Stanić-Vučinić, Dragana, "An improved method for isolation and purification of native bovine beta-lactoglobulin; separation of A and B beta-lactoglobulin isoforms" in Allergy, 66 (2011):523-524,
https://hdl.handle.net/21.15107/rcub_cherry_1473 .

TY  - JOUR
AU  - Stanić, Dragana
AU  - Monogioudi, Evanthia
AU  - Dilek, Ercili
AU  - Radosavljević, Jelena
AU  - Atanasković-Marković, Marina
AU  - Vučković, Olga
AU  - Raija, Lantto
AU  - Mattinen, Maija
AU  - Buchert, Johanna
AU  - Ćirković-Veličković, Tanja
PY  - 2010
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1126
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-V C H Verlag Gmbh, Weinheim
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 Vučković, 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-V C H Verlag Gmbh, Weinheim",
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., Vučković, 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-V C H Verlag Gmbh, Weinheim., 54(9), 1273-1284.
https://doi.org/10.1002/mnfr.200900184

Stanić D, Monogioudi E, Dilek E, Radosavljević J, Atanasković-Marković M, Vučković 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, Vučković, 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 . .