Angiotensin I-converting enzyme inhibitory properties of lentil protein hydrolysates: Determination of the kinetics of inhibition

被引：130

作者：

Barbana, Chockry ^{[1
]}

Boye, Joyce Irene ^{[1
]}

机构：

[1] Agr & Agri Food Canada, Ctr Food Res & Dev, St Hyacinthe, PQ J2S 8E3, Canada

来源：

FOOD CHEMISTRY | 2011年 / 127卷 / 01期

关键词：

ACE inhibitory activity; Bioactivity; Lentil protein hydrolysates; Lineweaver-Burk; WHEY-PROTEIN; PEPTIDES; CHICKPEA; PEA; DIGESTION; ASSAY;

D O I：

10.1016/j.foodchem.2010.12.093

中图分类号：

O69 [应用化学];

学科分类号：

070301 [无机化学];

摘要：

ACE inhibitory activity was studied for different hydrolysates obtained from protein concentrates of two lentil varieties by in vitro gastrointestinal simulation, Alcalase/Flavourzyme, papain and bromelain. Protein/peptide profiles studied by electrophoresis and HPLC-SEC showed a rich composition of the hydrolysates in small peptides ranging in size from 0.244 to 1.06 kDa. ACE inhibitory activity was measured using the HPLC Hippuryl-His-Leu (HHL) substrate method. Significantly different (P < 0.05) IC50 values ranging between 0.053 and 0.190 mg/ml were obtained for different hydrolysates. Furthermore, the inhibition mechanism investigated using Lineweaver-Burk plots revealed a non-competitive inhibition of ACE with inhibitor constants (K-i) between 0.16 and 0.46 mg/ml. These results demonstrate that hydrolysates of lentil proteins obtained by different enzymatic digestions may contain bioactive components. Crown Copyright (C) 2010 Published by Elsevier Ltd. All rights reserved.

引用

页码：94 / 101

页数：8

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