Journal
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
Volume 64, Issue 15, Pages 3054-3061Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.jafc.6b00314
Keywords
gelation; digestibility; myofibrillar protein; covalent cross-linking; phenolic antioxidants; gallic acid
Funding
- Oversea Study Fellowship from the China Scholarship Council (CSC)
- National Natural Science Foundation, China [31301497]
- USDA National Institute of Food and Agriculture, USA [1005724]
- NIFA [1005724, 812255] Funding Source: Federal RePORTER
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The dose-dependent effects of gallic acid (GA; at 0, 6, 30, and 150 mu mol/g protein) on chemical changes and gelling properties of oxidatively stressed porcine myofibrillar protein (MP) and in vitro digestibility of the gels were investigated. The incorporation of GA suppressed lipid oxidation and protein carbonyl formation but promoted the loss of thiol and amine groups, destabilization of the tertiary structure, aggregation, and cross-linking. The gelling potential (storage modulus) of MP was increased by nearly 50% with 6 and 30 mu mol/g of GA, corresponding to enhanced protein unfolding and aggregation and formation of disulfide-dominant covalent bonds. However, GA at 150 mu mol/g induced macroscopic aggregations and insolubility of MP, resulting in poorly structured gels. Despite the oxidative changes, MP gels did not show reduced susceptibility to digestive enzymes in vitro.
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