Journal
FOOD CHEMISTRY
Volume 293, Issue -, Pages 529-536Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2019.05.018
Keywords
Gallic acid; Myofibrillar protein; Glucose oxidase; Gelation; Meat
Funding
- National Key R&D Program of China [2018YFD0401203]
- USDA National Institute of Food and Agriculture, United States [1005724]
- NIFA [1005724, 812255] Funding Source: Federal RePORTER
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The effect of glucose oxidase (GOx) catalytic oxidation on the efficacy of gallic acid (GA) to modify the chemical structure and gelling behavior of myofibrillar protein (MP) was investigated. In contrast to non-oxidized MP samples where GA induced very little changes, GA (0, 6, 30, and 60 mu mol/g MP) under GOx treatment promoted sulfhydryl and amine loss (up to 58% and 49%, respectively). The attenuation of intrinsic tryptophan fluorescence in the GA/GOx-treated MP corroborated the finding. The gelling capacity of MP, corresponding to disulfide and non-disulfide bond formation in protein aggregates, was markedly enhanced by 60 mu mol GA under GOx, up to 86% in gel storage modulus G' and 53% in gel strength. The GOx-aided GA modification of MP could be a potential ingredient strategy in meat processing to promote textural attributes of cooked products.
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