Improvement of functional properties of chickpea proteins by hydrolysis with immobilised Alcalase

被引：142

作者：

del Mar Yust, Maria ^{[1
]}

Pedroche, Justo ^{[1
]}

del Carmen Millan-Linares, Maria ^{[1
]}

Maria Alcaide-Hidalgo, Juan ^{[1
]}

Millan, Francisco ^{[1
]}

机构：

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

来源：

FOOD CHEMISTRY | 2010年 / 122卷 / 04期

关键词：

Immobilised Alcalase; Functional properties; Chickpea hydrolysates; PERFORMANCE LIQUID-CHROMATOGRAPHY; MULTIPOINT COVALENT ATTACHMENT; GLYOXYL-AGAROSE SUPPORTS; FOAMING PROPERTIES; WHEY PROTEINS; STABILIZATION; PRODUCTS; ENZYMES; ACID; GELS;

D O I：

10.1016/j.foodchem.2010.03.121

中图分类号：

O69 [应用化学];

学科分类号：

081704 ;

摘要：

Limited chickpea protein hydrolysates ranging from 1% to 10% degree of hydrolysis were produced from chickpea protein isolate (CPI) using Alcalase immobilised on glyoxyl-agarose gels. Alcalase-glyoxyl derivative produced after 2411 of immobilisation at room temperature was 24 times more stable than soluble enzyme and presented approximately 51% of the activity of Alcalase. The chemical composition of chickpea hydrolysates were very close to that of CPI. Solubility, oil absorption, emulsifying activity and stability, and foaming capacity and stability were determined. All protein hydrolysates showed higher solubility than intact proteins, especially at pHs near isoelectric point of native chickpea proteins. Moreover, all hydrolysates had better functional properties, except emulsifying activity, than the original protein isolate. (C) 2010 Elsevier Ltd. All rights reserved.

引用

页码：1212 / 1217

页数：6

共 35 条

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