Obtaining of Brassica carinata protein hydrolysates enriched in bioactive peptides using immobilized digestive proteases

被引：63

作者：

Pedroche, J. ^{[1
]}

Yust, M. M. ^{[1
]}

Lqari, H. ^{[1
]}

Megias, C. ^{[1
]}

Giron-Calle, J. ^{[1
]}

Alaiz, M. ^{[1
]}

Vioque, J. ^{[1
]}

Millan, F. ^{[1
]}

机构：

[1] CSIC, Inst Grasa, Seville 41012, Spain

来源：

FOOD RESEARCH INTERNATIONAL | 2007年 / 40卷 / 07期

关键词：

Brassica carinata; immobilized enzymes; protein hydrolysates; bioactive peptides; ALDEHYDE-AGAROSE GELS; ANGIOTENSIN-CONVERTING ENZYME; ANTIOXIDANT ACTIVITY; INHIBITORY PEPTIDES; COVALENT ATTACHMENT; BETA-LACTOGLOBULIN; ACTIVE PEPTIDES; SOYBEAN PROTEIN; AMINO-ACIDS; STABILIZATION;

D O I：

10.1016/j.foodres.2007.04.001

中图分类号：

TS2 [食品工业];

学科分类号：

0832 ;

摘要：

Brassica carinata protein hydrolysates were obtained by sequential hydrolysis with immobilized trypsin, chymotrypsin, and carboxypeptidase A on glioxyl-agarose supports. The final protein hydrolysate with a 36% degree of hydrolysis was made up of peptides smaller than 15 kDa. Three peptide fractions were obtained after gel filtration chromatography and antioxidative, hypocholesterolemic, and inhibitory of angiotensin converting enzyme activities were assayed in comparison with the starting materials (protein isolate and hydrolysate). Total protein hydrolysate achieved the best results in the reduction of micellar cholesterol and fraction 11, composed by peptides between 1800 and 1400 Da, showed the best antioxidant and inhibitory of angiotensin converting enzyme activities. These results show that R carinata seed proteins may represent an useful source of bioactive peptides after hydrolysis with digestive proteases such as trypsin, chymotrypsin, and carboxypeptidase A. (c) 2007 Elsevier Ltd. All rights reserved.

引用

页码：931 / 938

页数：8

共 37 条

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