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Gelation properties of myofibrillar protein under malondialdehyde‐induced oxidative stress
Author(s) -
Wang Lin,
Zhang Min,
Fang Zhongxiang,
Bhandari Bhesh
Publication year - 2016
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.7680
Subject(s) - myofibril , chemistry , malondialdehyde , covalent bond , oxidative stress , oxidative phosphorylation , fourier transform infrared spectroscopy , protein aggregation , disulfide bond , food chemistry , biophysics , biochemistry , chromatography , organic chemistry , chemical engineering , catalysis , reaction mechanism , green chemistry , engineering , biology
BACKGROUND The structure of myofibrillar protein ( MP ) can be readily altered by oxidation, leading to the unfolding of MP structure, which further promotes protein–protein interactions, and thus influences the MP gelling properties. The objective of the study was to investigate the effect of malondialdehyde‐induced oxidative stress on the gelation properties of myofibrillar protein ( MP ). Structural changes of the oxidised MPs were evaluated by the contents of carbonyl and total sulfhydryls, surface hydrophobicity, SDS‐PAGE and Fourier transform infrared spectroscopy. The oxidative stability of the MP gels as indicated by lipid hydroperoxide was also determined. RESULTS With the addition of an MDA concentration less than 10 mmol L −1 , the MP gels showed an improved elasticity, gel strength, water holding capacity, and oxidative stability. Nevertheless, higher MDA concentration (25–50 mmol L −1 ) significantly reduced the gel quality, probably due to the formation of excessive covalent bonds in the system. CONCLUSION Results suggested that protein aggregation occurred in the oxidised system. Myosin was involved in gel formation through non‐disulfide covalent bond. © 2016 Society of Chemical Industry