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ACE-inhibitory peptides identified from the muscle protein hydrolysate of hard clam (Meretrix lusoria)

Paper ID Volume ID Publish Year Pages File Format Full-Text
35572 45096 2008 5 PDF Available
Title
ACE-inhibitory peptides identified from the muscle protein hydrolysate of hard clam (Meretrix lusoria)
Abstract

The meat of hard clam was extracted using hot water. The residual meat was freeze-dried then hydrolyzed at 50 °C for 5 h by Protamex (PX). The inhibitory effects of hot water extract and hydrolysate against angiotensin I converting enzyme (ACE) were investigated. The IC50 value of hot water extract and hydrolysate on ACE were 1.090 and 0.036 mg/ml, respectively. The PX hydrolysate was separated into five fractions by size exclusion chromatography on a Sephadex G-25 column. The fifth fraction of the hydrolysate having molecular weight ranged 350–300 Da showed the highest inhibitory efficiency ratio (IER) being 5831%/(mg ml). The amino acid sequence of the inhibitory peptide was Tyr-Asn (IC50 = 51 μM). The hydrolysate showed mixed-type inhibition kinetics while Captopril, the positive control, showed competitive inhibition on ACE. Their Ki values were 0.027 mg/ml and 0.0067 μg/ml, respectively.

Keywords
ACE-inhibitory peptide; Hard clam; Protein hydrolysate; Angiotensin I converting enzyme; Inhibition type; Gel filtration
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ACE-inhibitory peptides identified from the muscle protein hydrolysate of hard clam (Meretrix lusoria)
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Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 43, Issue 7, July 2008, Pages 743–747
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us