PURIFICATION AND PROPERTIES OF A HIGH-AFFINITY L-2-HALOACID DEHALOGENASE FROM AZOTOBACTER SP STRAIN RC26

Authors
DIEZ A PRIETO NI ALVAREZ MJ BAUTISTA JM PUYET A GARRIDOPERTIERRA A
Citation
A. Diez et al., PURIFICATION AND PROPERTIES OF A HIGH-AFFINITY L-2-HALOACID DEHALOGENASE FROM AZOTOBACTER SP STRAIN RC26, Letters in applied microbiology, 23(5), 1996, pp. 279-282
Citations number
22
Categorie Soggetti
Microbiology,"Biothechnology & Applied Migrobiology
Journal title
Letters in applied microbiology → ACNP
ISSN journal
02668254
Volume
23
Issue
5
Year of publication
1996
Pages
279 - 282
Database
ISI
SICI code
0266-8254(1996)23:5<279:PAPOAH>2.0.ZU;2-9
Abstract
A monomeric 29 kDa protein showing dehalogenase activity on several ha logenated carboxylic acids has been purified from Azotobacter sp. stra in RC26. The purified enzyme is specific for the L isomer of optically active 2-haloacids leading to the inversion of the product configurat ion. The dehalogenase is active at temperatures ranging from 30 to 60 degrees C and shows a relatively high affinity for the substrate. The combined thermal stability, high substrate affinity and resistance to enzyme inhibitors found for the RC26 dehalogenase may be relevant for its use as catalyst in biotransformation processes.