Study on the mechanism of mulberry polyphenols inhibiting oxidation of beef myofibrillar protein

Abstract In order to explore the mechanism of mulberry polyphenols inhibiting the oxidation of myofibrillar protein (MP), the effect of mulberry polyphenols on the structure and physicochemical properties of MP in the oxidation system was investigated. The results revealed that the content of carbonyl group and sulfhydryl group of MP was notably reduced, while the Zeta potential, storage modulus G' and surface hydrophobicity were improved when the addition of mulberry polyphenol was 0.5%. SDS-PAGE showed an irreducible aggregation of mulberry polyphenols with proteins. Fluorescence spectroscopy and FT-IR analysis manifested that mulberry polyphenols promoted the unfolding of protein structure and the transformation of α-helix to β-turn structure. Scanning electron microscopy (SEM) observed that oxidation with polyphenols facilitated the cross-linking and aggregation of MP more tightly. Nevertheless, excessive addition (≥1.0%) weakened its gel properties. Thus, to maintain the good quality of meat products, both polyphenols addition and oxidation intensity should be controlled simultaneously.