Protein degradation and peptide formation with antioxidant activity in pork protein extracts inoculated with Lactobacillus plantarum and Staphylococcus simulans

Abstract

This study focused on sarcoplasmic and myofibrillar protein degradation and the formation of peptides with antioxidant activity by mixed starters (Lactobacillus plantarum CD101 and Staphylococcus simulans NJ201). Gel electrophoresis indicated that the mixed starters can hydrolyze both sarcoplasmic and myofibrillar proteins, and the concentration of peptides increased (P < .05). Compared with the control group, using mixed starters led to a significant increase (P < .05) in the DPPH radical scavenging activity, Fe2+ chelating activity, and ABTS radical scavenging activity of sarcoplasmic proteins, but demonstrated no significant difference in myofibrillar proteins. Two hydrophobic fractions (C2, C5) separated by RP-HPLC in the inoculation groups with sarcoplasmic proteins showed high DPPH radical scavenging activity (66.60%, 60.50%). Eighteen peptides were identified by LC-MS/MS, which mainly arose from triosephosphate isomerase, creatine kinase M-type, and glyceraldehyde-3-phosphate dehydrogenase. Hydrophobic amino acids accounted for a large proportion. Our results indicate that mixed starters affect proteolytic characterization and contribute to the formation of peptides with antioxidant capacity in sarcoplasmic proteins.