Abstract
A pilot-scale production was developed to produce oligopeptide powder from black-bone silky fowl (Gallus gallus domesticus Brisson) muscle (BSFP) by two-step enzymatic hydrolysis and multistage separation. The resultant BSFP was assessed for antioxidant activities against four free radicals (hydroxyl, 1,1-dipheny-2-picrylhydrazyl (DPPH), superoxide and peroxyl) and against the peroxidation of linoleic acid in a lipid peroxidation model system. After separation by reversed-phase high-performance liquid chromatography (RP-HPLC), five major fractions of BSFP were tested for DPPH radical scavenging activity and subjected to mass spectrometry to identify the active peptides. BSFP showed potential antioxidant activity in four assay systems. Three RP-HPLC fractions produced higher antioxidant effect than BSFP, with Fraction 4 showing the strongest activity. A total of 18 peptides were identified, and two peptides - Leu-Trp-Arg and Asn-Met - had strong scavenging activity, with IC50 values of 2.28 ± 0.05 and 4.65 ± 0.09 mg mL(-1) , respectively. Asn-Met is a novel antioxidative peptide that has not been previously reported. The results showed that the pilot-scale production of BSFP was a practical way to produce peptides with high value and potential antioxidant activity. BSFP and its antioxidative peptides can be a source of natural antioxidant and used as a food additive.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
