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 . .