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Changes in the structure, digestibility and immunoreactivities of glycinin induced by the cross‐linking of microbial transglutaminase following heat denaturation
Author(s) -
Yang Anshu,
Xia Jiaheng,
Gong Yuqing,
Deng Han,
Wu Zhihua,
Li Xin,
Tong Ping,
Chen Hongbing
Publication year - 2017
Publication title -
international journal of food science and technology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.831
H-Index - 96
eISSN - 1365-2621
pISSN - 0950-5423
DOI - 10.1111/ijfs.13507
Subject(s) - tissue transglutaminase , denaturation (fissile materials) , chemistry , polyacrylamide gel electrophoresis , food science , biochemistry , protein secondary structure , electrophoresis , gel electrophoresis , enzyme , nuclear chemistry
Summary This study aimed to evaluate the effects of microbial transglutaminase ( MTG )‐mediated modification on the structure, digestibility and immunoreactivities of glycinin. Glycinin was separated from soya bean and cross‐linked with MTG , and the sulphate‐polyacrylamide gel electrophoresis ( SDS ‐ PAGE ) showed that the molecular weight of cross‐linked glycinin was higher than that of native glycinin. Individual MTG cross‐linking could maintain stable secondary structures and spatial structure. Sequential heat denaturation and MTG cross‐linking could promote the unfolding of protein structures and reduce their hydrophobicity. The digestibility of glycinin was decreased, and its immunoreactivities were increased because of MTG ‐induced structural alteration, including primary and spatial structures.