The proteomics homology of antioxidant peptides extracted from dry-cured Xuanwei and Jinhua ham. (15th November 2018)

• Record Type: Journal Article
• Authors: Xing, Lujuan; Liu, Rui; Gao, Xiaoge; Zheng, Jinxiao; Wang, Chong; Zhou, Guanghong; Zhang, Wangang
• Is Part Of: Food chemistry. Volume 266(2018)
• Page Start: 420
• Page End: 426
• Publication Date: 2018-11-15
• Subjects: Jinhua ham -- Xuanwei ham -- Antioxidant activity -- Peptide -- Protein homology; Food -- Analysis -- Periodicals; Food -- Composition -- Periodicals; 664
• DOI: 10.1016/j.foodchem.2018.06.034
• Languages: English
• ISSNs: 0308-8146

Abstract

Highlights: The purification of XHP and JHP showed that low molecular weight peptides (<1000 Da) had better antioxidant activity. Peptide composition and homologous proteins were matched to confirm the sequences of antioxidant peptide. Myosin, troponin and actin mainly accounted for the generation of abundant peptides in both Xuanwei and Jinhua ham. Abstract: The objective of this study was to investigate the antioxidant activity and the homology of peptides extracted from dry-cured Xuanwei and Jinhua ham. The antioxidant activity of crude peptides was assessed by ORAC and ABTS assays and the scavenging effects on DPPH and O 2− free radicals. LC-ESI-Q-TOF-MS/MS was used to analyze the peptide composition. Based on the identified peptides, homologous proteins were matched by the Peaks software. Overall, 243 and 213 peptides were identified with their parent proteins in Xuanwei and Jinhua dry-cured hams. Based on the ORAC and TEAC values, XHP showed higher antioxidant ability than JHP ( P < 0.05). After further purification by G-15 chromatography, the results indicate that the oligopeptides with less than 1000 Da had greater antioxidant activity than the other two fractions. Homology-based proteomics showed that the majority of peptides originated from myosin which accounted for 26% in XHP and 32% in JHP respectively.