Isolation and identification of antioxidative peptides from pilot-scale black-bone silky fowl (Gallus gallus domesticus Brisson) muscle oligopeptides


Correspondence to: Muyi Cai, China National Research Institute of Food and Fermentation Industries, Beijing 100027, People's Republic of China. E-mail:



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. © 2013 Society of Chemical Industry