A mutant subtilisin E with remarkably thermostability is reported. It is mo
re active against the typical substrate s-AAPF-pna than the wild-type subti
lisin E. The time required for getting 50% residual activity of Ser236Cys s
ubtilisin E at 60 degrees C in aqueous solution was approximately 80 min wh
ich is 4 times longer than that of wild-type subtilisin E. Similar to the w
ild-type subtilisin E, the amidase activity of Ser236Cys subtilisin E is dr
amatically reduced in the presence of dimethylformamide (DMF).