甲酸脱氢酶
格式化
NAD+激酶
辅因子
丙酮
化学
溶剂
甲醇
基质(水族馆)
热稳定性
甲酸钠
色谱法
酶
生物化学
催化作用
有机化学
生物
生态学
作者
Haitao Ding,D.-F. Liu,Z.-L. Li,Yi‐Ling Du,Xiaohong Xu,Yong Zhao
标识
DOI:10.1111/j.1365-2672.2011.05124.x
摘要
To characterize a robust NAD(+) -dependent formate dehydrogenase firstly obtained from a nonmethylotroph, Bacillus sp. F1.The Bacillus sp. F1 NAD(+) -dependent formate dehydrogenase (BacFDH) gene was cloned by TAIL-PCR and heterologous expressed in Escherichia coli. BacFDH was stable at temperatures below 55°C, and the half-life at 60°C was determined as 52·9 min. This enzyme also showed a broad pH stability and retained more than 80% of the activities after incubating in buffers with different pH ranging from 4·5 to 10·5 for 1 h. The activity of BacFDH was significantly enhanced by some metal ions. Moreover, BacFDH exhibited high tolerance to 20% dimethyl sulfoxide, 60% acetone, 10% methanol, 20% ethanol, 60% isopropanol and 20% n-hexane. Like other FDHs, BacFDH displayed strict substrate specificity for formate.We isolated a robust formate dehydrogenase, designated as BacFDH, which showed excellent thermal stability, organic solvent stability and a broad pH stability.The multi-aspect stability makes BacFDH a competitive candidate for coenzyme regeneration in practical applications of chiral chemicals and pharmaceuticals synthesis with a relatively low cost, especially for the catalysis performed in extreme pH conditions and organic solvents.
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