Angiotensin I-converting enzyme inhibitory activity of chickpea and pea protein hydrolysates

被引：128

作者：

Barbana, Chockry ^{[1
]}

Boye, Joyce Irene ^{[1
]}

机构：

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

来源：

FOOD RESEARCH INTERNATIONAL | 2010年 / 43卷 / 06期

关键词：

ACE inhibitory activity; Bioactivity; Chickpea; Enzymatic digestion; Pea; WHEY-PROTEIN; FUNCTIONAL-PROPERTIES; BIOACTIVE PEPTIDES; PURIFICATION; BITTERNESS; DIGESTION; ISOLATE; L;

D O I：

10.1016/j.foodres.2010.05.003

中图分类号：

TS2 [食品工业];

学科分类号：

100403 [营养与食品卫生学];

摘要：

CE inhibitory activity was studied for different hydrolysates obtained from protein concentrates of chickpea (kabuli and desi) and yellow pea (Golden) using in vitro gastrointestinal simulation, alcalase/flavourzyme, and papain. Protein/peptide profiles studied by SOS-PAGE and SE-HPLC, showed a rich composition of the hydrolysates in small peptides having MWs under 4 kDa. Papain hydrolysed yellow pea proteins showed the highest ACE inhibitory activity. In addition, chickpea desi proteins hydrolysed by in vitro gastrointestinal simulation showed higher ACE inhibition (IC50 of 140 +/- 1 mu g/ml) compared to its digests obtained by alcalase/flavourzyme (IC50 of 228 +/- 3 mu g/m1) or papain (IC50 of 180 +/- 1 mu/ml) ;and to chickpea kabuli hydrolysed by gastrointestinal simulation (IC50 of 229 +/- 1 mu/ml). The results demonstrate that enzymatic hydrolysates of chickpea and pea proteins contain bioactive ACE inhibitory peptides; furthermore, the type of enzyme used for hydrolysis affects the ACE inhibitory activity. Crown Copyright (C) 2010 Published by Elsevier Ltd. All rights reserved.

引用

页码：1642 / 1649

页数：8

共 36 条

[1]

Structural analysis of new antihypertensive peptides derived from cheese whey protein by proteinase K digestion [J].

Abubakar, A ;

Saito, T ;

Kitazawa, H ;

Kawai, Y ;

Itoh, T .

JOURNAL OF DAIRY SCIENCE, 1998, 81 (12) :3131-3138

[2]

DETERMINATION OF THE DEGREE OF HYDROLYSIS OF FOOD PROTEIN HYDROLYSATES BY TRINITROBENZENESULFONIC ACID [J].

ADLERNISSEN, J .

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 1979, 27 (06) :1256-1262

[3]

*AGR AGR FOOD CAN, 2008, STAT OV CAN PULS IND

[4]

Effects of heat treatment and in vitro digestion on the Angiotensin converting enzyme inhibitory activity of some legume species [J].

Akillioglu, H. Guel ;

Karakaya, Sibel .

EUROPEAN FOOD RESEARCH AND TECHNOLOGY, 2009, 229 (06) :915-921

[5]

Aluko RE, 2008, J AOAC INT, V91, P947

[6]

*AOAC, 1995, OFF METH AN 992 15

[7]

Comparison of the functional properties of pea, chickpea and lentil protein concentrates processed using ultrafiltration and isoelectric precipitation techniques [J].

Boye, J. I. ;

Aksay, S. ;

Roufik, S. ;

Ribereau, S. ;

Mondor, M. ;

Farnworth, E. ;

Rajamohamed, S. H. .

FOOD RESEARCH INTERNATIONAL, 2010, 43 (02) :537-546

[8]

Angiotensin I-converting enzyme inhibitory properties and SDS-PAGE of red lentil protein hydrolysates [J].

Boye, Joyce Irene ;

Roufik, Samira ;

Pesta, Noemie ;

Barbana, Chockry .

LWT-FOOD SCIENCE AND TECHNOLOGY, 2010, 43 (06) :987-991

[9]

Purification of angiotensin I-converting enzyme inhibitory peptides and antihypertensive effect of milk produced by protease-facilitated lactic fermentation [J].

Chen, Guan-Wen ;

Tsai, Jenn-Shou ;

Pan, Bonnie Sun .

INTERNATIONAL DAIRY JOURNAL, 2007, 17 (06) :641-647

[10]

Anti-hypertensive Nutraceuticals and Functional Foods [J].

Chen, Zhen-Yu ;

Peng, Cheng ;

Jiao, Rui ;

Wong, Yin Mei ;

Yang, Nan ;

Huang, Yu .

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 2009, 57 (11) :4485-4499

← 1 2 3 4 →