枯草芽孢杆菌
生物化学
生物合成
严格的回应
鸟氨酸
精氨酸
甘氨酸
生物催化
氨基酸
化学
异源表达
异源的
生物
细菌
基因
重组DNA
大肠杆菌
催化作用
遗传学
离子液体
作者
Kun Yan,Rongzhen Tian,Linpei Zhang,Xueqin Lv,Long Liu,Yanfeng Liu
出处
期刊:Fermentation
[MDPI AG]
日期:2022-03-07
卷期号:8 (3): 116-116
被引量:2
标识
DOI:10.3390/fermentation8030116
摘要
Guanidinoacetate (GAA) is a naturally occurring amino acid derivative and the direct precursor of creatine, which is widely used in feed additives and the pharmaceutical industry. The current industrial synthesis of GAA is based on chemical methods, which limits the application of GAA. Here, a biological approach is developed for food safety GAA production via whole-cell biocatalysis by the generally regarded as safe (GRAS) bacterium Bacillus subtilis. First, we introduced a heterologous arginine: glycine amidinotransferase (AgaT) from Amycolatopsis kentuckyensis into B. subtilis and optimized its expression level using strategies including: promoter optimization, ribosome binding site (RBS) and N-terminal coding sequence (NCS) screening. In order to alleviate the waste of arginine and the inhibition of AgaT by ornithine, we optimized the natural ornithine cycle in B. subtilis. At the same time, the first gene in the glycine degradation pathway was knocked out. After optimization using these strategies, the titer of GAA was 4.26 g/L with a productivity of 0.21 g/L/h in 20 h, which provides a new method for the biosynthesis of GAA.
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