| Literature DB >> 25977033 |
Abir Mokni Ghribi1, Ines Maklouf Gafsi1, Assaâd Sila2, Christophe Blecker3, Sabine Danthine3, Hamadi Attia1, Ali Bougatef4, Souhail Besbes5.
Abstract
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 ∼ 66.5 mN m(-1) for CPI to ∼ 59.1 m Nm(-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.Entities:
Keywords: Chickpea protein isolates; Conformation; Enzymatic hydrolysis; Functional properties
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Year: 2015 PMID： 25977033 DOI： 10.1016/j.foodchem.2015.04.109
Source DB: PubMed Journal: Food Chem ISSN： 0308-8146 Impact factor: 7.514