Peanut protein structure, polyphenol content and immune response to peanut proteins

In vivo are modulated by laccase

L. Mihajlovic, J. Radosavljevic, E. Nordlund, M. Krstic, T. Bohn, J. Smit, J. Buchert, T. Cirkovic Velickovic (Corresponding Author)

Research output: Contribution to journalArticleScientificpeer-review

5 Citations (Scopus)

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 < 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 < 0.05) and reduced IL-13 secretion in in vitro cultured splenocytes 7 fold (p < 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.

Original languageEnglish
Pages (from-to)2357-2366
Number of pages10
JournalFood and Function
Volume7
Issue number5
DOIs
Publication statusPublished - 1 May 2016
MoE publication typeA1 Journal article-refereed

Fingerprint

peanut protein
Laccase
laccase
Polyphenols
protein structure
polyphenols
immune response
peanuts
crosslinking
Proteins
proteins
allergens
bioavailability
Food
circular dichroism spectroscopy
isorhamnetin
Allergens
Biological Availability
food allergies
extracts

Cite this

Mihajlovic, L., Radosavljevic, J., Nordlund, E., Krstic, M., Bohn, T., Smit, J., ... Cirkovic Velickovic, T. (2016). Peanut protein structure, polyphenol content and immune response to peanut proteins: In vivo are modulated by laccase. Food and Function, 7(5), 2357-2366. https://doi.org/10.1039/c5fo01325a
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. In: Food and Function. 2016 ; Vol. 7, No. 5. pp. 2357-2366.
@article{639878d7a6c246dca5d70ccfbef61cee,
title = "Peanut protein structure, polyphenol content and immune response to peanut proteins: In vivo are modulated by laccase",
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 < 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 < 0.05) and reduced IL-13 secretion in in vitro cultured splenocytes 7 fold (p < 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.",
author = "L. Mihajlovic and J. Radosavljevic and E. Nordlund and M. Krstic and T. Bohn and J. Smit and J. Buchert and {Cirkovic Velickovic}, T.",
year = "2016",
month = "5",
day = "1",
doi = "10.1039/c5fo01325a",
language = "English",
volume = "7",
pages = "2357--2366",
journal = "Food and Function",
issn = "2042-6496",
publisher = "Royal Society of Chemistry RSC",
number = "5",

}

Mihajlovic, L, Radosavljevic, J, Nordlund, E, Krstic, M, Bohn, T, Smit, J, Buchert, J & Cirkovic Velickovic, T 2016, 'Peanut protein structure, polyphenol content and immune response to peanut proteins: In vivo are modulated by laccase', Food and Function, vol. 7, no. 5, pp. 2357-2366. https://doi.org/10.1039/c5fo01325a

Peanut protein structure, polyphenol content and immune response to peanut proteins : In vivo are modulated by laccase. / Mihajlovic, L.; Radosavljevic, J.; Nordlund, E.; Krstic, M.; Bohn, T.; Smit, J.; Buchert, J.; Cirkovic Velickovic, T. (Corresponding Author).

In: Food and Function, Vol. 7, No. 5, 01.05.2016, p. 2357-2366.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Peanut protein structure, polyphenol content and immune response to peanut proteins

T2 - In vivo are modulated by laccase

AU - Mihajlovic, L.

AU - Radosavljevic, J.

AU - Nordlund, E.

AU - Krstic, M.

AU - Bohn, T.

AU - Smit, J.

AU - Buchert, J.

AU - Cirkovic Velickovic, T.

PY - 2016/5/1

Y1 - 2016/5/1

N2 - 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 < 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 < 0.05) and reduced IL-13 secretion in in vitro cultured splenocytes 7 fold (p < 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.

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 < 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 < 0.05) and reduced IL-13 secretion in in vitro cultured splenocytes 7 fold (p < 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.

UR - http://www.scopus.com/inward/record.url?scp=84971350141&partnerID=8YFLogxK

U2 - 10.1039/c5fo01325a

DO - 10.1039/c5fo01325a

M3 - Article

VL - 7

SP - 2357

EP - 2366

JO - Food and Function

JF - Food and Function

SN - 2042-6496

IS - 5

ER -