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Activity and enantioselectivity of wildtype and lid mutated Candida rugosa lipase isoform 1 in organic solvents
Author(s) -
Secundo Francesco,
Carrea Giacomo,
Tarabiono Chiara,
Brocca Stefania,
Lotti Marina
Publication year - 2004
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.20034
Subject(s) - candida rugosa , lipase , chemistry , enzyme , gene isoform , active site , catalysis , vinyl acetate , methanol , organic chemistry , enzyme assay , stereochemistry , biochemistry , gene , copolymer , polymer
The activity and enantioselectivity of lipase 1 from Candida rugosa and of a chimera enzyme obtained by replacing the lid of isoform 1 with the lid of isoform 3 were compared in organic solvents. The alcoholysis of chloro ethyl 2‐hydroxy hexanoate with methanol and of vinyl acetate with 6‐methyl‐5‐hepten‐2‐ol were used as model reactions in different reaction conditions. The chimera enzyme was less active and enantioselective than the wildtype in all the conditions tested. A rationale for such decreases could be that the chimera lipase has a lower proportion of enzyme molecules in the open form. This might lead to a hindered access to the enzyme active site, thus affecting the catalytic activity. © 2004 Wiley Periodicals, Inc.