Immobilization of pig muscle aldolase on a silica-based support |
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Authors: | L. Horváth Magdolna Ábrahám L. Boross B. Szajáni |
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Affiliation: | Department of Biochemistry, Attila József University, Szeged, Hungary. |
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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. |
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Keywords: | KeywordHeading" >Index Entries Aldolase, immobilized pig muscle aldolase support, silica-based catalytic properties, immobilized aldolase stability tests, immobilized aldolase D-fructose 1,6-diphosphate splitting enzyme reactor |
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