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BioMed Research International
Volume 2014, Article ID 438459, 8 pages
http://dx.doi.org/10.1155/2014/438459
Research Article

Angiotensin I Converting Enzyme Inhibitory Peptides Obtained after In Vitro Hydrolysis of Pea (Pisum sativum var. Bajka) Globulins

Department of Biochemistry and Food Chemistry, University of Life Sciences, Ulica Skromna 8, 20-704 Lublin, Poland

Received 13 February 2014; Revised 26 June 2014; Accepted 22 July 2014; Published 28 August 2014

Academic Editor: Blanca Hernández-Ledesma

Copyright © 2014 Anna Jakubczyk and Barbara Baraniak. 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.

Abstract

Pea seeds represent a valuable source of active compounds that may positively influence health. In this study, the pea globulins were digested in vitro under gastrointestinal condition and potentially bioaccessible angiotensin I converting enzyme (ACE) inhibitory peptides were identified. The degree of hydrolysis after pepsin, 14.42%, and pancreatin, 30.65%, were noted. The peptides with the highest ACE inhibitory properties were separated using ion exchange chromatography on DEAE-cellulose. Thirteen peptides fractions were obtained but only four showed potential antihypertensive properties. The highest inhibitory activity was determined for the fraction F8 (IC50 = 0.0014 mg/mL). This fraction was separated on Sephadex G10 and two peptide fractions were obtained. The peptides fraction (B) with the highest ACE inhibitory activity (IC50 = 0.073 mg/mL) was identified by ESI-MS/MS. The sequences of ACE inhibitory peptides were GGSGNY, DLKLP, GSSDNR, MRDLK, and HNTPSR. Based on Lineweaver-Burk plots for the fraction B, the kinetic parameters as , , and and mode of inhibition were determined. This fraction belongs to uncompetitive inhibitor of ACE activity. The seeds of pea are the source of precursor protein, which releases the ACE inhibitory peptides as a result of enzymatic hydrolysis.