Research Article | OPEN ACCESS
Study on Optimal Conditions of Alcalase Enzymatic Hydrolysis of Soybean Protein Isolate
1Yongsheng Ma, 2Xianhui Sun and 1Lintong Wang
1Chemistry and Chemical Engineering and Environment Engineering College, Weifang University, Weifang, Shandong 261061, P.R. China
2Agricultural Engineering College, Weifang Vocation College, Weifang, Shandong 261041, P.R. China
Advance Journal of Food Science and Technology 2015 2:154-158
Received: February ‎13, ‎2015 | Accepted: March ‎1, ‎2015 | Published: August 05, 2015
Abstract
Soybean protein isolate was hydrolyzed to obtain soybean polypeptide solution using Alcalase as hydrolase. Degree of hydrolysis and the recovery rate of protein were used to characterize the soybean protein hydrolysis reaction result. Influence factors of soybean protein hydrolysis reaction including the substrate concentration, temperature, pH, enzyme concentration characterized by E/S (ratio of Enzyme and Substrate) and hydrolysis time were systematically studied with single factor and multi-level experimental. The optimal reaction conditions of soybean protein isolate hydrolyzed by Alcalase were that the substrate concentration was 8%; E/S was 3.6 AU/100 g substrate; pH was 8.0; temperature was 60°C and hydrolysis time was 2 h. The study also showed that the hydrolytic activity of the Alcalase to soybean protein isolate was stronger in the front 1 h; the hydrolytic activity of Alcalase weakened gradually with time when reaction time was longer than 2 h.
Keywords:
Alcalase, optimal hydrolysis conditions, soybean polypeptide, soybean protein isolate,
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Competing interests
The authors have no competing interests.
Open Access Policy
This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.
Copyright
The authors have no competing interests.
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