Abstract
Peanut hydrolysate obtained after 6 h of digestion by Alcalase was used to isolate angiotensin I converting enzyme (ACE) inhibitory peptides. After centrifugation and ultrafiltration through a 0.2 microm nylon filter, the hydrolysate was filtered through the polyethersulfone membrane with a molecular weight cutoff (MWCO) of 10 kDa. The resulting permeate was then separated by primary reverse-phase high performance liquid chromatography (RP-HPLC). Eluate was divided into six major fractions according to eluation time. The fraction with eluting time 50-60 min showed the most potent ACE inhibition and was subjected to further purification by the secondary RP-HPLC. Four peaks were found to have strong ACE inhibitory activities, and their IC(50) values were determined. Peptide mass for the most potent peak was obtained by matrix-assisted laser desorption and ionization (MALDI), and sequence was determined by MALDI tandem TOF-TOF (time-of-flight) mass spectrometer (MS/MS) to be Lys-Ala-Phe-Arg.
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.
