High pressure, thermal and pulsed electric-field-induced structural changes in selected food allergens
Article first published online: 21 JUN 2010
Copyright © 2010 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Molecular Nutrition & Food Research
Volume 54, Issue 12, pages 1701–1710, December 2010
How to Cite
Johnson, P. E., Van der Plancken, I., Balasa, A., Husband, F. A., Grauwet, T., Hendrickx, M., Knorr, D., Mills, E. N. C. and Mackie, A. R. (2010), High pressure, thermal and pulsed electric-field-induced structural changes in selected food allergens. Mol. Nutr. Food Res., 54: 1701–1710. doi: 10.1002/mnfr.201000006
- Issue published online: 2 DEC 2010
- Article first published online: 21 JUN 2010
- Manuscript Accepted: 6 MAY 2010
- Manuscript Revised: 26 APR 2010
- Manuscript Received: 7 JAN 2010
- European Commission through the NovelQ project. Grant Number: FOOD-CT-2005-015710
- UK Biological and Biotechnological Sciences Research Council through a Strategic Programme Grant to IFR
- High pressure;
- Pulsed electric field
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.