Evolution of antioxidant peptides and their proteomic homology during processing of Jinhua ham

作者：Li, Ping; Xu, Feiran; Zhou, Hui^*; Gao, Yafei; Zhu, Hanlin; Nie, Wen; Wang, Zhaoming; Wang, Ying; Deng, Jieying; Zhou, Kai; Xu, Baocai

来源：Food Science and Technology, 2022, 166: 113771.

DOI：10.1016/j.lwt.2022.113771

• Jinhua ham
• Antioxidant peptides
• Size-exclusion chromatography
• Protease activities
• Protein homology

This study aimed to clarify the evolution of antioxidant peptides and their proteomic homology during a continuous period of Jinhua ham processing. The peptide content increased during the process, reaching a value of 1.92% (weight %, based on meat weight) in ham at the end of dry-ripening, which was approximately 8-fold higher than that prior to salting. From scavenging effects on 1,1-diphenyl-2-picrylhydrazyl radical (DPPH center dot) and hydroxyl radical (center dot OH) and chelating ability on Fe2+, it was suggested that peptides generated at the end of dry -ripening had the highest level of antioxidant activity. Size-exclusion chromatography indicated that the anti -oxidation of peptides might be related to their MWs, where more fractions with small MWs result in higher antioxidant activity. The results of endogenous protease activities showed 22.33% of the initial activities of Cathepsin B were retained, suggesting that Cathepsin B plays a key role in the formation of antioxidant peptides. Homology-based proteomics showed that peptides primarily arose from myosin (32.37%), followed by actin (16.91%), troponin T (12.08%) and others.