Enzymatic hydrolysis and their effects on conformational and functional properties of peanut protein isolate |
| |
Authors: | Guanli Zhao Yan Liu Mouming Zhao Jiaoyan Ren Bao Yang |
| |
Affiliation: | 1. College of Light Industry and Food Science, South China University of Technology, Guangzhou 510640, China;2. South China Botanical Garden, Chinese Academy of Sciences, Guangzhou 510650, China |
| |
Abstract: | The effects of limited enzymatic hydrolysis by Alcalase on the conformational and functional properties of peanut (Arachis hypogaea L.) protein isolate (PPI) were investigated. Acid subunits of arachin were most susceptible to Alcalase hydrolysis, followed by conarachin and the basic subunits of arachin. Enzymatic hydrolysis increased the thermal stability of arachin and led to a sharp increase in the number of disulphide bonds with a decrease of the sulphydryl group in PPI hydrolysates in comparison with PPI. The analysis of intrinsic fluorescence spectra indicated a more moveable tertiary conformation of PPI hydrolysates than PPI. The limited emzymatic hydrolysis improved the functional properties of PPI, such as protein solubility and gel-forming ability, but impaired the emulsifying activity index. |
| |
Keywords: | Peanut protein isolate Enzymatic hydrolysis Functional property Conformation |
本文献已被 ScienceDirect 等数据库收录! |