Chymotryptic hydrolysates of α-kafirin, the storage protein of sorghum (Sorghum bicolor) exhibited angiotensin converting enzyme inhibitory activity

被引：53
作者：
Kamath, Vasudeva
Niketh, Sajeeda
Chandrashekar, Arun
Rajini, P. S. [1 ]
机构：
[1] Cent Food Technol Res Inst, Food Protectants & Infestat Control Dept, Mysore 570020, Karnataka, India
[2] Cent Food Technol Res Inst, Plant Cell Biotechnol Dept, Mysore 570020, Karnataka, India
来源：
FOOD CHEMISTRY | 2007年 / 100卷 / 01期
关键词：
sorghum flour; angiotensin converting enzyme; kafirin; chymotryptic hydrolysate; IC50; Lineweaver-Burk plots;
D O I：
10.1016/j.foodchem.2005.10.004
中图分类号：
O69 [应用化学];
学科分类号：
081704 ;
摘要：
Kafirin is the main storage protein (prolamin) in sorghum grains. a-Kafirin, the alcohol soluble fraction, was isolated from sorghum flour. Treatment of a-kafirin with chymotrypsin yielded a hydrolysate which on fractionation, using Sephadex G-25 column, yielded four fractions with significant angiotensin converting enzyme (ACE) inhibitory activity in vitro. The IC50 values of these fractions ranged from 1.3 to 24.3 mu g/ml. Two of the fractions were found to be competitively inhibiting the enzyme, while two other fractions were non-competitive inhibitors. These results demonstrate that chymotryptic hydrolysates of sorghum prolamin could serve as a good source of peptides with angiotensin I converting enzyme inhibitory activity. (c) 2005 Elsevier Ltd. All rights reserved.
引用
收藏
页码：306 / 311
页数：6
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