Genetic engineering for enhanced production of a novel alkaline protease BSP-1 in Bacillus amyloliquefaciens
文献类型： 外文期刊
作者： Jiang, Cong 1 ; Ye, Changwen 2 ; Liu, Yongfeng 3 ; Huang, Kuo 2 ; Jiang, Xuedeng 1 ; Zou, Dian 1 ; Li, Lu 4 ; Han, Wenyuan 1 ; Wei, Xuetuan 1 ;
作者机构： 1.Huazhong Agr Univ, State Key Lab Agr Microbiol, Hubei Hongshan Lab, Wuhan, Peoples R China
2.China Natl Tobacco Corp, Zhengzhou Tobacco Res Inst, Zhengzhou, Peoples R China
3.GeneMind Biosci Co Ltd, Shenzhen, Peoples R China
4.Guangdong Acad Agr Sci, Sericultural & Argi Food Res Inst, Key Lab Funct Foods, Minist Agri & Rural Affairs,Guangdong Key Lab Agr, Guangzhou, Peoples R China
关键词： alkaline protease; bacillus amyloliquefaciens; promoter screening; recombinant expression; fermentation optimization
期刊名称：FRONTIERS IN BIOENGINEERING AND BIOTECHNOLOGY （ 影响因子：6.064； 五年影响因子：6.303 ）
ISSN： 2296-4185
年卷期： 2022 年 10 卷
页码：
收录情况： SCI
摘要： Alkaline protease has been widely applied in food, medicine, environmental protection and other industrial fields. However, the current activity and yield of alkaline protease cannot meet the demand. Therefore, it is important to identify new alkaline proteases with high activity. In this study, we cloned a potential alkaline protease gene bsp-1 from a Bacillus subtilis strain isolated in our laboratory. BSP-1 shows the highest sequence similarity to subtilisin NAT (S51909) from B. subtilis natto. Then, we expressed BSP-1 in Bacillus amyloliquefaciens BAX-9 and analyzed the protein expression level under a collection of promoters. The results show that the P43 promoter resulted in the highest transcription level, protein level and enzyme activity. Finally, we obtained a maximum activity of 524.12 U/mL using the P43 promoter after fermentation medium optimization. In conclusion, this study identified an alkaline protease gene bsp-1 from B. subtilis and provided a new method for high-efficiency alkaline protease expression in B. amyloliquefaciens.
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