Abstract

Flavonoids, a significant subclass of polyphenols, possess antioxidant properties and contribute to the preservation of chilled meat. In this paper, a phosphate buffer solution (pH = 6.25, simulated chilled pork) and a Fenton oxidation system (simulated myofibrillar protein oxidation process during storage) were established to explain the antioxidative preservation of chilled pork using peanut shell flavonoids (PSFs). The results indicated that PSFs changed the secondary structure of myofibrillar protein (MP), significantly inhibiting the oxidation of amino acids and the formation of carbonyl groups in MP (P < 0.05). Because PSFs and amino acids in chilled pork were combined to form complex through non-covalent bond in a pH 6.25 environment and covalent bond in a Fenton oxidation system. The antioxidant capacity of the complex was significantly enhanced (P < 0.05). The molecular docking technique predicted the antioxidant binding sites were Cys176, Ala182 and Val 124. This study provides a theoretical foundation for the preservation of chilled pork using PSFs.

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