Abstract
Black-bone silky fowl (Gallus gallus domesticus Brisson) muscle was hydrolyzed with Alcalase 2.4L and papain, and treated by multistage separation. The black-bone silky fowl muscle peptides (BSFP) with low molecular weight obtained was tested for antioxidant and angiotensin I-converting enzyme (ACE) inhibitory activities. BSFP was then separated by reversed-phase high performance liquid chromatography. Five major fractions were collected and their 2,2′-azinobis (3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) radical scavenging and ACE inhibitory activities were assayed. Fractions 3–5 displaying higher activities were subjected to mass spectrometry to identify the active peptides. A total of 29 peptide sequences were identified, and 11 peptides were synthesized for further ABTS radical scavenging and ACE inhibitory activity analysis. Finally, one potent antioxidative peptide (Leu-Trp-Arg, 3.25±0.11mmol Trolox equivalents/g sample) and two novel potent ACE inhibitory peptides (Leu-Glu-Arg, IC50=45.62±2.40μM; Gly-Ala-Gly-Pro, IC50=253.07±6.66μM) were found. Their activities were approximately 6.9, 14.1 and 2.8 times higher than that of BSFP, respectively.
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.
