High pressure, thermal and pulsed electric-field-induced structural changes in selected food allergens

Phil E. Johnson; Iesel Van Der Plancken; Ana Balasa; Fiona A. Husband; Tara Grauwet; Marc Hendrickx; Dietrich Knorr; E. N Clare Mills; Alan R. Mackie

doi:10.1002/mnfr.201000006

High pressure, thermal and pulsed electric-field-induced structural changes in selected food allergens

Phil E. Johnson, Iesel Van Der Plancken, Ana Balasa, Fiona A. Husband, Tara Grauwet, Marc Hendrickx, Dietrich Knorr, E. N Clare Mills, Alan R. Mackie

Research output: Contribution to journal › Article › peer-review

Abstract

Scope: The effects of high-pressure/temperature treatment and pulsed electric field treatment on native peanut Ara h 2, 6 and apple Mal d 3 and Mal d 1b prepared by heterologous expression were examined.Methods and results: Changes in secondary structure and aggregation state of the treated proteins were characterized by circular dichroism spectroscopy and gel-filtration chromatography. Pulsed electric field treatment did not induce any significant changes in the structure of any of the allergens. High-pressure/temperature at 20°C did not change the structure of the Ara h 2, 6 or Mal d 3 and resulted in only minor changes in structure of Mal d 1b. Ara h 2, 6 was stable to HPP at 80°C, whereas changes in circular dichroism spectra were observed for both apple allergens. However, these changes were attributable to aggregation and adiabatic heating during HPP. An ELISA assay of temperature treated Mal d 3 showed the antibody reactivity correlated well with the loss of structure.Conclusion: In conclusion, novel-processing techniques had little effect on purified allergen structure. Further studies will demonstrate if these stability properties are retained in foodmatrices. Copyright © 2010 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

Original language	English
Pages (from-to)	1701-1710
Number of pages	9
Journal	Molecular Nutrition and Food Research
Volume	54
Issue number	12
DOIs	https://doi.org/10.1002/mnfr.201000006
Publication status	Published - Dec 2010

Keywords

Allergy
Apple
High pressure
Peanut
Pulsed electric field

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1002/mnfr.201000006

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title = "High pressure, thermal and pulsed electric-field-induced structural changes in selected food allergens",

abstract = "Scope: The effects of high-pressure/temperature treatment and pulsed electric field treatment on native peanut Ara h 2, 6 and apple Mal d 3 and Mal d 1b prepared by heterologous expression were examined.Methods and results: Changes in secondary structure and aggregation state of the treated proteins were characterized by circular dichroism spectroscopy and gel-filtration chromatography. Pulsed electric field treatment did not induce any significant changes in the structure of any of the allergens. High-pressure/temperature at 20°C did not change the structure of the Ara h 2, 6 or Mal d 3 and resulted in only minor changes in structure of Mal d 1b. Ara h 2, 6 was stable to HPP at 80°C, whereas changes in circular dichroism spectra were observed for both apple allergens. However, these changes were attributable to aggregation and adiabatic heating during HPP. An ELISA assay of temperature treated Mal d 3 showed the antibody reactivity correlated well with the loss of structure.Conclusion: In conclusion, novel-processing techniques had little effect on purified allergen structure. Further studies will demonstrate if these stability properties are retained in foodmatrices. Copyright {\textcopyright} 2010 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.",

keywords = "Allergy, Apple, High pressure, Peanut, Pulsed electric field",

author = "Johnson, {Phil E.} and {Van Der Plancken}, Iesel and Ana Balasa and Husband, {Fiona A.} and Tara Grauwet and Marc Hendrickx and Dietrich Knorr and Mills, {E. N Clare} and Mackie, {Alan R.}",

year = "2010",

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doi = "10.1002/mnfr.201000006",

language = "English",

volume = "54",

pages = "1701--1710",

journal = "Molecular Nutrition and Food Research",

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publisher = "John Wiley & Sons Ltd",

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TY - JOUR

T1 - High pressure, thermal and pulsed electric-field-induced structural changes in selected food allergens

AU - Johnson, Phil E.

AU - Van Der Plancken, Iesel

AU - Balasa, Ana

AU - Husband, Fiona A.

AU - Grauwet, Tara

AU - Hendrickx, Marc

AU - Knorr, Dietrich

AU - Mills, E. N Clare

AU - Mackie, Alan R.

PY - 2010/12

Y1 - 2010/12

N2 - Scope: The effects of high-pressure/temperature treatment and pulsed electric field treatment on native peanut Ara h 2, 6 and apple Mal d 3 and Mal d 1b prepared by heterologous expression were examined.Methods and results: Changes in secondary structure and aggregation state of the treated proteins were characterized by circular dichroism spectroscopy and gel-filtration chromatography. Pulsed electric field treatment did not induce any significant changes in the structure of any of the allergens. High-pressure/temperature at 20°C did not change the structure of the Ara h 2, 6 or Mal d 3 and resulted in only minor changes in structure of Mal d 1b. Ara h 2, 6 was stable to HPP at 80°C, whereas changes in circular dichroism spectra were observed for both apple allergens. However, these changes were attributable to aggregation and adiabatic heating during HPP. An ELISA assay of temperature treated Mal d 3 showed the antibody reactivity correlated well with the loss of structure.Conclusion: In conclusion, novel-processing techniques had little effect on purified allergen structure. Further studies will demonstrate if these stability properties are retained in foodmatrices. Copyright © 2010 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

AB - Scope: The effects of high-pressure/temperature treatment and pulsed electric field treatment on native peanut Ara h 2, 6 and apple Mal d 3 and Mal d 1b prepared by heterologous expression were examined.Methods and results: Changes in secondary structure and aggregation state of the treated proteins were characterized by circular dichroism spectroscopy and gel-filtration chromatography. Pulsed electric field treatment did not induce any significant changes in the structure of any of the allergens. High-pressure/temperature at 20°C did not change the structure of the Ara h 2, 6 or Mal d 3 and resulted in only minor changes in structure of Mal d 1b. Ara h 2, 6 was stable to HPP at 80°C, whereas changes in circular dichroism spectra were observed for both apple allergens. However, these changes were attributable to aggregation and adiabatic heating during HPP. An ELISA assay of temperature treated Mal d 3 showed the antibody reactivity correlated well with the loss of structure.Conclusion: In conclusion, novel-processing techniques had little effect on purified allergen structure. Further studies will demonstrate if these stability properties are retained in foodmatrices. Copyright © 2010 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

KW - Allergy

KW - Apple

KW - High pressure

KW - Peanut

KW - Pulsed electric field

U2 - 10.1002/mnfr.201000006

DO - 10.1002/mnfr.201000006

M3 - Article

C2 - 20568235

SN - 1613-4125

VL - 54

SP - 1701

EP - 1710

JO - Molecular Nutrition and Food Research

JF - Molecular Nutrition and Food Research

IS - 12

ER -

High pressure, thermal and pulsed electric-field-induced structural changes in selected food allergens

Abstract

Keywords

UN SDGs

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