Abstract
This experiment was designed to evaluate the influence of mulberry polyphenols (MP) on oxidation stability of sarcoplasmic and myofibrillar proteins in dried minced pork slice during processing and storage. Composition, amino acid side chain modification, average particle size, hydrophobicity and solubility of proteins in the slices were investigated. MP displayed protective effects on oxidation stability of sarcoplasmic and myofibrillar proteins in slices, considering carbonyl formation and transformation from SH group to SS group were remarkably retarded by MP. Proteins in MP-treated slices possessed larger average particle size but lower aggregation during processing and storage. Meanwhile, the strengthened ionic bonds and weakened hydrogen, hydrophobic and disulfide bond could be responsible for the improved protein stability of slice with MP. All these results suggested that mulberry polyphenol could improve protein oxidation stability in meat products.
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