Effects of enzymatic hydrolysis on conformational and functional properties of chickpea protein isolate

被引:261
|
作者
Ghribi, Abir Mokni [1 ]
Gafsi, Ines Maklouf [1 ]
Sila, Assaad [2 ,3 ]
Blecker, Christophe [4 ]
Danthine, Sabine [4 ]
Attia, Hamadi [1 ]
Bougatef, Ali [2 ]
Besbes, Souhail [1 ]
机构
[1] Univ Sfax, Ecole Natl Ingenieurs Sfax, Lab Anal Valorisat & Secur Aliments, Sfax 3038, Tunisia
[2] Univ Sfax, Ecole Natl Ingenieurs Sfax, Unite Enzymes & Bioconvers, Sfax 3038, Tunisia
[3] Univ Lille 1, Inst Reg Rech Agroalimentaire & Biotechnol Charle, EA1026, Equipe ProBioGEM, F-59655 Villeneuve Dascq, France
[4] Univ Liege, Gembloux Agro BioTech, Unite Technol Ind Agroalimentaires, B-5030 Gembloux, Belgium
关键词
Chickpea protein isolates; Enzymatic hydrolysis; Conformation; Functional properties; AMINO-ACID-COMPOSITION; EMULSIFYING PROPERTIES; ANTIOXIDANT ACTIVITY; BETA-LACTOGLOBULIN; SUNFLOWER PROTEIN; FOOD PROTEINS; SOLUBILITY; LENTIL;
D O I
10.1016/j.foodchem.2015.04.109
中图分类号
O69 [应用化学];
学科分类号
081704 ;
摘要
The impact of enzymatic hydrolysis by Alcalase on the conformational and functional properties of chickpea protein isolate (CPI) was investigated. The physicochemical, interfacial tension and surface characteristics of CPI and their hydrolysates (CPH) according to the degree of hydrolysis (DH) were also determined. These parameters were then related to the changes in the emulsification activity (EAI) and stability (ESI). The enzymatic hydrolysis was found to improve protein recovery and solubility, leading to a reduction in the molecular weight bands with a concomitant increase in the intensity and appearance of protein bands having apparent molecular mass below 20 kDa. The interfacial tension decreased from similar to 66.5 mN m(-1) for CPI to similar to 59.1 mN m(-1) for CPH. A similar trend was observed for the surface charge which declined from -27.55 mV to -16.4 mV for the CPI and CPH, respectively. These changes were found to have a detrimental effect on the EAI and ESI values. (C) 2015 Elsevier Ltd. All rights reserved.
引用
收藏
页码:322 / 330
页数:9
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