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Modification of the reaction system of Ara h 2 catalyzed by MTGase: Products and reaction conditions analysis
Author(s) -
Wu Zhihua,
Zhao Ruifang,
Ren Linmei,
Li Xin,
Yang Anshu,
Tong Ping,
Chen Hongbing
Publication year - 2018
Publication title -
journal of food processing and preservation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.511
H-Index - 48
eISSN - 1745-4549
pISSN - 0145-8892
DOI - 10.1111/jfpp.13422
Subject(s) - deamidation , chemistry , intramolecular force , maillard reaction , intermolecular force , catalysis , residue (chemistry) , biochemistry , organic chemistry , enzyme , molecule
Peanut ( Arachis hypogaea ) is listed among the eight major food allergens, in which Ara h 2 is the major allergen. The microbial transglutaminase (MTGase)‐catalyzed cross‐linking reaction reduces the allergenicity of Ara h 2. However, deamidation might occur and influence the cross‐linking reaction. In this work, native and reduced Ara h 2 were catalyzed by MTGase. In addition to intermolecular cross‐linking, intramolecular cross‐linking and deamidation were proven to occur simultaneously. Moreover, intramolecular cross‐linking sites were identified using mass spectrometry and the PLINK software. The reactions moved toward different directions because of different reduction conditions and different protein concentrations. Practical applications Cross‐linking is a common processing method used to improve the textural and functional properties of protein. Deamidation reaction might occur during processing and influence the cross‐linking reaction. The two types of reactions have a competitive relation, because both of them occur on glutamine residue. In Ara h 2 and MTGase system, protein concentration and reduction content influence the direction of reaction. The results can be applied to modify the reaction system of Ara h 2 catalyzed by MTGase. In addition, the relationship between structure and properties changes on Ara h 2 was discussed based on analysis of cross‐linking sites.