Peanut protein structure, polyphenol content and immune response to peanut proteins in vivo are modulated by laccase
Само за регистроване кориснике
2016
Аутори
Mihajlović, L.Radosavljević, Jelena
Nordlund, Emilia
Krstić-Ristivojević, Maja
Bohn, Torsten
Smit, Joost
Buchert, Johanna
Ćirković-Veličković, Tanja
Чланак у часопису (Објављена верзија)
Метаподаци
Приказ свих података о документуАпстракт
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.
Извор:
Food and Function, 2016, 7, 5, 2357-2366Издавач:
- Royal Soc Chemistry, Cambridge
Финансирање / пројекти:
- Молекуларне особине и модификације неких респираторних и нутритивних алергена (RS-MESTD-Basic Research (BR or ON)-172024)
- Reinforcement of the Faculty of Chemistry, University of Belgrade, towards becoming a Center of Excellence in the region of WB for Molecular Biotechnology and Food research (EU-FP7-256716)
- European Academy for Allergy and Clinical Immunology
- European Academy for Allergy and Clinical Immunology, COST Action [FA1005]
Напомена:
- Supplementary material: http://cherry.chem.bg.ac.rs/handle/123456789/3591
DOI: 10.1039/c5fo01325a
ISSN: 2042-6496
PubMed: 27138276
WoS: 000377136900025
Scopus: 2-s2.0-84971350141
Институција/група
Hemijski fakultet / Faculty of ChemistryTY - 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 . .