A mutant subtilisin E with enhanced thermostability
- Cite this article as:
- Yang, Y., Jiang, L., Yang, S. et al. World Journal of Microbiology and Biotechnology (2000) 16: 249. doi:10.1023/A:1008959825832
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A mutant subtilisin E with remarkably thermostability is reported. It is more active against the typical substrate s-AAPF-pna than the wild-type subtilisin E. The time required for getting 50% residual activity of Ser236Cys subtilisin E at 60 °C in aqueous solution was approximately 80 min which is 4 times longer than that of wild-type subtilisin E. Similar to the wild-type subtilisin E, the amidase activity of Ser236Cys subtilisin E is dramatically reduced in the presence of dimethylformamide (DMF).