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Updated: May 30, 2026

Hydrophobic Salt-modified Nafion for Enzyme Immobilization and Stabilization
Published on: July 11, 2012
Characterization of a thermally stable and organic solvent-adaptative NAD+ -dependent formate dehydrogenase from
1Institute of Microbiology, College of Life Science, Zhejiang University, Hangzhou, China.
Aims:
To characterize a robust NAD(+) -dependent formate dehydrogenase firstly obtained from a nonmethylotroph, Bacillus sp. F1.
Methods And Results:
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.
Conclusion:
We isolated a robust formate dehydrogenase, designated as BacFDH, which showed excellent thermal stability, organic solvent stability and a broad pH stability.
Significance And Impact Of The Study:
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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