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Mar. Drugs 2016, 14(6), 110; doi:10.3390/md14060110

Identification of Angiotensin I-Converting Enzyme Inhibitory Peptides Derived from Enzymatic Hydrolysates of Razor Clam Sinonovacula constricta

1
School of Life Sciences and Food Technology, Hanshan Normal University, Chaozhou 521041, China
2
College of Biosystems Engineering and Food Science, Zhejiang University, Hangzhou 310058, China
3
School of Chemistry and Environmental Engineering, Hanshan Normal University, Chaozhou 521041, China
4
National Institute of Food Science & Technology, University of Agriculture, Faisalabad 38040, Pakistan
*
Author to whom correspondence should be addressed.
Academic Editor: Se-Kwon Kim
Received: 11 April 2016 / Revised: 23 May 2016 / Accepted: 30 May 2016 / Published: 3 June 2016
(This article belongs to the Special Issue Marine Proteins and Peptides)
View Full-Text   |   Download PDF [2255 KB, uploaded 3 June 2016]   |  

Abstract

Angiotensin I-converting enzyme (ACE) inhibitory activity of razor clam hydrolysates produced using five proteases, namely, pepsin, trypsin, alcalase, flavourzyme and proteases from Actinomucor elegans T3 was investigated. Flavourzyme hydrolysate showed the highest level of degree of hydrolysis (DH) (45.87%) followed by A. elegans T3 proteases hydrolysate (37.84%) and alcalase (30.55%). The A. elegans T3 proteases was observed to be more effective in generating small peptides with ACE-inhibitory activity. The 3 kDa membrane permeate of A. elegans T3 proteases hydrolysate showed the highest ACE-inhibitory activity with an IC50 of 0.79 mg/mL. After chromatographic separation by Sephadex G-15 gel filtration and reverse phase-high performance liquid chromatography, the potent fraction was subjected to MALDI/TOF-TOF MS/MS for identification. A novel ACE-inhibitory peptide (VQY) was identified exhibiting an IC50 of 9.8 μM. The inhibitory kinetics investigation by Lineweaver-Burk plots demonstrated that the peptide acts as a competitive ACE inhibitor. The razor clam hydrolysate obtained by A. elegans T3 proteases could serve as a source of functional peptides with ACE-inhibitory activity for physiological benefits. View Full-Text
Keywords: ACE-inhibitory peptides; razor clam; enzymatic hydrolysis; Actinomucor elegans proteases; identification; MALDI/TOF-TOF MS/MS ACE-inhibitory peptides; razor clam; enzymatic hydrolysis; Actinomucor elegans proteases; identification; MALDI/TOF-TOF MS/MS
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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MDPI and ACS Style

Li, Y.; Sadiq, F.A.; Fu, L.; Zhu, H.; Zhong, M.; Sohail, M. Identification of Angiotensin I-Converting Enzyme Inhibitory Peptides Derived from Enzymatic Hydrolysates of Razor Clam Sinonovacula constricta. Mar. Drugs 2016, 14, 110.

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