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Immobilization of pig muscle aldolase on a silica-based support
L Horváth1, M Abrahám, L Boross
1Department of Biochemistry, Attila József University, Szeged, Hungary.
Applied Biochemistry and Biotechnology
|December 1, 1989
Abstract:
Pig muscle aldolase was covalently attached to a silica-based support possessing aldehyde functional groups. The activity of the immobilized enzyme was 37 U/g solid, and the specific activity calculated on a bound protein basis was 1.9 U/mg protein. The optimum pH for the catalytic activity was pH 7.5. The apparent optimum temperature was found to be 45 degrees C. The Km app value of the immobilized aldolase with D-fructose 1,6-diphosphate as substrate was 1.25 X 10(-4) M. The conformational stability was improved by the immobilization. The immobilized aldolase was used for the continuous splitting of D-fructose 1,6-diphosphate.