In:
Journal of the Science of Food and Agriculture, Wiley, Vol. 100, No. 1 ( 2020-01-15), p. 308-314
Abstract:
Peanut is among the most common of food allergies, and one of its allergens is Ara h 2. A previous study revealed that this allergen was recognized by serum immunoglobulin E (IgE) in over 90% of a peanut‐allergic patient population. Enzymatic cross‐linking is a popular processing method used to tailor food functionality, such as antigenicity. RESULT The cross‐linking reactions of Ara h 2 were catalyzed by polyphenol oxidase (PPO), and the relevant reaction sites were identified using mass spectrometry and StavroX software. Two pairs of intramolecular cross‐linking peptides and two intermolecular cross‐linking peptides were found. Intramolecular cross‐linking was speculated to occur between ARG 131 (amino acids 116–131) and TYR 65 (amino acids 63–80) and between TYR 60 (amino acids 56–62) and ARG 92 (amino acids 92–102); the intermolecular cross‐linking sites were ARG 31 with TYR 84 or TYR 89 and TYR 65 or TYR 72 with ARG 92 or ARG 102 . Three out of four cross‐linking peptides were found in α‐helices, and destruction of this secondary structure resulted in a loose tertiary structure. Although seven linear allergen epitopes were involved in cross‐linking, the IgE binding capacity of protein changed slightly, while its sensitization potential decreased in mouse model. CONCLUSION Exploring the structural change of Ara h 2 after cross‐linking is beneficial in further understanding the influence of structure on sensitization. This result indicated the future possibility of precision processing on structure of proteins to improve their properties. © 2019 Society of Chemical Industry
Type of Medium:
Online Resource
ISSN:
0022-5142
,
1097-0010
Language:
English
Publisher:
Wiley
Publication Date:
2020
detail.hit.zdb_id:
2001807-1
