Antioxidative and antihypertensive bioactive peptides were successfully derived from Parkia speciosa seed using alcalase. The effects of temperature (25 and 50 °C), substrate-to-enzyme ratio (S/E ratio, 20 and 50), and incubation time (0.5, 1, 2 and 5h) were evaluated based on 2,2-diphenyl-1-picrylhydrazyl (DPPH), ferric reducing antioxidant power (FRAP) and angiotensin-converting enzyme (ACE) assays. Bioactive peptide extracted at a hydrolysis condition of: temperature=50 °C, S/E ratio=50 and incubation time=2h, exhibited the highest DPPH radical scavenging activity (2.9 mg GAE/g), reducing power (11.7 mM) and %ACE-inhibitory activity (80.2%). The sample was subsequently subjected to fractionation and the peptide fraction of <10 kDa showed the strongest bioactivities. A total of 29 peptide sequences from peptide fraction of <10 kDa were identified as the most potent contributors to the bioactivities. These novel bioactive peptides were suggested to be beneficial to nutraceutical and food industries.
* Title and MeSH Headings from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.