Abstract
Hypertension is a threatening chronic disease, which become a global killer among the adult population. The mortality rate increasing day by day even several Angiotensin I-converting enzyme (ACE) inhibitor drugs were introduced. Bioactive peptides derived from aquatic resources exhibits potential ACE inhibitory activity. The objective of this work is to report the purification and molecular docking studies of angiotensin-I converting enzyme (ACE) inhibitory peptide isolated from shortfin scad (Decapterus macrosoma) waste protein hydrolysate (SWH), enzymatically prepared by using alcalase. The purification process included ultrafiltration, gel filtration and reverse phase high performance liquid chromatography (RP-HPLC). Results showed that ultra-filtered peptide fraction (< 3kDa) possessed the highest ACE inhibitory activity, followed by the fraction 14 by gel filtration. Fraction P obtained by RP-HPLC, with the amino acid sequence of RGVGPVPAA (IC50 = 0.20mg/ml) was identified. In terms of ACE inhibition, the Lineweaver-Burk plot showed that the SWH peptide obtained acted as a competitive ACE inhibitor. The molecular docking studies showed that the SWH peptide exhibit hydrogen bonds and Pi-interactions with ACE by Z-dock scores. These results showed that the purified peptide isolated from shortfin scad waste hydrolysate has potential antihypertensive properties which could potentially be used as functional food ingredients.
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.
