Premium
Acylation of subtilisin with long fatty acyl residues affects its activity and thermostability in aqueous medium
Author(s) -
Plou Francisco J.,
Ballesteros Antonio
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)80415-x
Subject(s) - thermostability , subtilisin , acylation , chemistry , aqueous solution , thermal stability , organic chemistry , enzyme , catalysis
Subtilisin Carlsberg has been artificially hydrophobized by acylation with octanoyl or palmitoyl chlorides. Samples with several degrees of substitution were obtained. Hydrophobization facilitates in some cases the binding of synthetic or natural substrates. Furthermore, derivatized subtilisins show improved thermal stability (15‐fold at 45°C) in aqueous solution. As a result, octanoyl‐subtilisin exhibits enhanced thermostability without losing biological activity.