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Purification and properties of a high‐affinity L‐2‐haloacid dehalogenase from Azotabacter sp. strain RC26
Author(s) -
Diez A.,
Prieto M.I.,
Alvarez M.J.,
Bautista J.M.,
Puyet A.,
Pertierra Garrido
Publication year - 1996
Publication title -
letters in applied microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.698
H-Index - 110
eISSN - 1472-765X
pISSN - 0266-8254
DOI - 10.1111/j.1472-765x.1996.tb00189.x
Subject(s) - dehalogenase , biotransformation , enzyme , active site , biochemistry , strain (injury) , substrate (aquarium) , chemistry , stereochemistry , biology , anatomy , ecology
A monomeric 29 kDa protein showing dehalogenase activity on several halogenated carboxylic acids has been purified from Azotobacter sp. strain RC26. The purified enzyme is specific for the L isomer of optically active 2‐haloacids leading to the inversion of the product configuration. The dehalogenase is active at temperatures ranging from 30 to 60d̀C 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.