Improved catalytic performance of a 2-haloacid dehalogenase from Azotobacter sp. by ion-exchange immobilisation.

Abstract:

:The stability and catalytic efficacy of the L-2-haloacid dehalogenase isolated from Azotobacter sp. RC26 were studied after immobilisation on a DEAE Sephacel solid matrix. While the optimum temperature for the soluble dehalogenase falls in the range of 30-40 degrees C, the activity of the immobilised enzyme shows a four-fold increase at 60 degree C. Immobilisation on a plug-flow bioreactor extends the range of usable substrate concentration. The improved catalytic characteristics after immobilisation of the haloacid dehalogenase may be relevant for its possible utilization in biotechnological applications ranging from waste treatment to synthesis of stereoisomers.

authors

Diez A,Prieto MI,Alvarez MJ,Bautista JM,Garrido J,Puyet A

doi

10.1006/bbrc.1996.0489

subject

Has Abstract

pub_date

1996-03-27 00:00:00

pages

828-33

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006291X96904891

journal_volume

220

pub_type

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