The beneficial effects of rutin on myofibrillar protein gel properties and related changes in protein conformation

Food Chemistry
Na JiaDengyong Liu

Abstract

Effects of different levels of rutin (0, 10, 50, 100 and 200 μmol/g protein) on the conformational changes and gel properties of myofibrillar protein (MP) were investigated. Rutin at 200 μmol/g caused the greatest carbonyl content. The incorporation of rutin caused the losses of thiol, free amine and α-helix contents, reduction in tryptophan intrinsic fluorescence intensity, and enhanced exposure of hydrophobic groups and protein cross-linking. When compared with control, the MP gels with 10, 50 and 100 μmol/g rutin had higher gel strength but slight lower water-holding capacity; the gels appeared to have compact microstructure with few visible pores. However, 200 μmol/g rutin was detrimental to gel properties. All the gels with rutin presented higher final storage modulus and converted to elasticity-dominant gel types. The results indicate that a slightly high concentration of rutin could improve MP gel properties which are related to the protein conformational changes induced by rutin.

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Citations

Dec 20, 2020·Comprehensive Reviews in Food Science and Food Safety·Xue ZhaoGuanghong Zhou

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