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碱性蛋白酶在[具体对象未提及]中的过表达及其从豆渣中回收蛋白质的潜在应用。

Overexpression of alkaline protease in and its potential application for recovery of protein from soybean dregs.

作者信息

Chen Hao, Wu Jie, Huang Xiaodan, Feng Xuzhong, Ji Hongwu, Zhao Liangzhong, Wang Jianrong

机构信息

College of Food and Chemical Engineering, Shaoyang University, Shaoyang, China.

Hunan Provincial Key Laboratory of Soybean Products Processing and Safety Control, Shaoyang, China.

出版信息

Front Microbiol. 2022 Aug 26;13:968439. doi: 10.3389/fmicb.2022.968439. eCollection 2022.

Abstract

Proteases are important for decomposition of proteins to generate peptides or amino acids and have a broad range of applications in different industries. Herein, a gene encoding an alkaline protease (AprBcp) from R1 was cloned and bioinformatics analyzed. In addition, a series of strategies were applied to achieve high-level expression of AprBcp in . The maximum activity of AprBcp reached 165,870 U/ml after 60 h fed-batch cultivation in 50 l bioreactor. The purified recombinant AprBcp exhibited maximum activity at 60°C and pH 10.0, and remained stable in the range from pH 8.0 to 11.0 and 30 to 45°C. Metal ions Ca, Mn, and Mg could improve the stability of AprBcp. Furthermore, the recombinant AprBcp displayed great potential application on the recovery of protein from soybean dregs. The results of this study will provide an effective method to prepare AprBcp in and its potential application on utilization of soybean dregs.

摘要

蛋白酶对于蛋白质分解以产生肽或氨基酸很重要,并且在不同行业有广泛应用。在此,克隆了来自R1的编码碱性蛋白酶(AprBcp)的基因并进行了生物信息学分析。此外,应用了一系列策略以在……中实现AprBcp的高水平表达。在50升生物反应器中进行60小时补料分批培养后,AprBcp的最大活性达到165,870 U/ml。纯化的重组AprBcp在60°C和pH 10.0时表现出最大活性,并且在pH 8.0至11.0以及30至45°C范围内保持稳定。金属离子Ca、Mn和Mg可以提高AprBcp的稳定性。此外,重组AprBcp在从豆渣中回收蛋白质方面显示出巨大的潜在应用。本研究结果将为在……中制备AprBcp提供一种有效方法及其在豆渣利用方面的潜在应用。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/27e8/9459226/2e677a3f51cd/fmicb-13-968439-g002.jpg

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