ISOLATION OF A HIGHLY ENANTIOSELECTIVE EPOXIDE HYDROLASE FROM RHODOCOCCUS SP NCIMB-11216

Authors
MISCHITZ M FABER K WILLETTS A
Citation
M. Mischitz et al., ISOLATION OF A HIGHLY ENANTIOSELECTIVE EPOXIDE HYDROLASE FROM RHODOCOCCUS SP NCIMB-11216, Biotechnology letters, 17(9), 1995, pp. 893-898
Citations number
16
Categorie Soggetti
Biothechnology & Applied Migrobiology
Journal title
Biotechnology letters → ACNP
ISSN journal
01415492
Volume
17
Issue
9
Year of publication
1995
Pages
893 - 898
Database
ISI
SICI code
0141-5492(1995)17:9<893:IOAHEE>2.0.ZU;2-O
Abstract
Whole cells of Rhodococcus sp. NCIMB 11216 catalyze the asymmetric hyd rolysis of racemic epoxides giving access to chiral epoxides and diols , which are important chiral building blocks for the, synthesis of bio active compounds. Employing a four-step purification procedure, the ep oxide hydrolase responsible for the reaction was isolated and characte rized to be a cofactor-independent, soluble monomeric protein of simil ar to 35kDa, exhibiting an isoelectric point of 4.7.