Angiotensin Converting Enzyme Inhibition with Antiradicalar Activity of Thornback Ray Gelatin Hydrolysate: Determination and Separation of Peptide Fractions
Journal Title: Journal of Hypertension and Management - Year 2017, Vol 3, Issue 1
Abstract
Bioactive peptides from collagen and gelatin with antioxidant and antihypertensive properties have become a topic of great interest for health and food preservation industries. Thornback Ray Skin Gelatin Hydrolysate with an hydrolysis degree of 9.23% was prepared by treatment with Alcalase (TRGH-Alcalase). The hydrolysate was found to exhibit ACE inhibitory activity and 1, 1-Diphenyl-2-Picrylhydrazyl (DPPH) scavenging activity with an IC50 values of 0.92 and > 5 mg/mL, respectively. The molecular weight distribution of the hydrolysate showed the abundance of small-sized peptides with average molecular weight below 1000 Da (57%) contrary to the untreated gelatin. The hydrolysate and the gelatin did not show hemolytic activity at a concentration of 2 mg/ml. TRGH-Alcalase was further fractionated by using size-exclusion chromatography. Fraction F3 showing the highest antioxidant and ACE inhibitory activity was further separated by Reversed-Phased High Performance Liquid Chromatography (RP-HPLC). Sub-fractions SF3 and SF9 had higher anti-ACE activity and SF5 had the highest antioxidant activity. Taken together, the results suggest that the hydrolysate as well as the peptide fractions could offer potential uses as a functional food.
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- EP ID EP344674
- DOI 10.23937/2474-3690/1510026
- Views 121
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