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.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Diez A,Prieto MI,Alvarez MJ,Bautista JM,Garrido J,Puyet Adoi
10.1006/bbrc.1996.0489subject
Has Abstractpub_date
1996-03-27 00:00:00pages
828-33issue
3eissn
0006-291Xissn
1090-2104pii
S0006291X96904891journal_volume
220pub_type
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