Improved catalytic performance of a 2-haloacid dehalogenase from Azotobacter sp. by ion-exchange immobilisation.
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.
Diez
A
A
Departmento de Bioquímica y Biología Molecular IV, Facultad de Veterinaria, Universidad Complutense de Madrid, Spain.
Prieto
M I
MI
Alvarez
M J
MJ
Bautista
J M
JM
Garrido
J
J
Puyet
A
A
D001395:Azotobacter / Q000201:enzymology*; D002384:Catalysis; D003636:DEAE-Cellulose; D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000378:metabolism*; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D006867:Hydrolases / Q000302:isolation & purification / Q000378:metabolism*; D007475:Ion Exchange Resins; D007700:Kinetics; D013816:Thermodynamics
D004800:Enzymes, Immobilized; D007475:Ion Exchange Resins; D003636:DEAE-Cellulose; D006867:Hydrolases; C034507:2-haloacid dehalogenase