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Immobilization of pig muscle aldolase on a silica-based support

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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°C. The Km app value of the immobilized aldolase with D-fructose 1,6-diphosphate as substrate was 1.25 ×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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Authors and Affiliations

  1. Department of Biochemistry, Attila József University, Szeged, Hungary

    L. Horváth, Magdolna Ábrahám & L. Boross

  2. Reanal Factory of Laboratory Chemicals, 1441 Budapest 70, PO Box 54, Hungary

    B. Szajáni

Authors
  1. L. Horváth
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  2. Magdolna Ábrahám
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  3. L. Boross
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  4. B. Szajáni
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Horváth, L., Ábrahám, M., Boross, L. et al. Immobilization of pig muscle aldolase on a silica-based support. Appl Biochem Biotechnol 22, 223–235 (1989). https://doi.org/10.1007/BF02921758

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  • DOI: https://doi.org/10.1007/BF02921758

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