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Characterization and comparison of soluble and immobilized pig muscle aldolases

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Abstract

Pig muscle aldolase was insolubilized by covalent attachment to a polyacrylamide matrix containing carboxylic functional groups. The catalytic activity of the Akrilex C-aldolase was 2014 units/g solid, i.e., an activity loss of only about 5% relative to the initial activity. The pH optimum for catalytic activity shifted form 7.25 to 7.5 and the apparent temperature optimum from 313 to 318 K. The Michaelis constant of the insolubilized enzyme was significantly higher than that of the soluble aldolase. Heat- and urea-inactivation experiments revealed that the immobilization increased the stability of the enzyme.

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Authors and Affiliations

  1. Department of Biochemistry, Attila József University, H-6726 Szeged, 52, Középfasor, Hungary

    Magdolna Ábrahám, Lóránt Horvth, Mária Simon, Béla Szajńi & Lászl Boross

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  1. Magdolna Ábrahám
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  2. Lóránt Horvth
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  3. Mária Simon
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  4. Béla Szajńi
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  5. Lászl Boross
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Ábrahám, M., Horvth, L., Simon, M. et al. Characterization and comparison of soluble and immobilized pig muscle aldolases. Appl Biochem Biotechnol 11, 91–100 (1985). https://doi.org/10.1007/BF02798541

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  • DOI: https://doi.org/10.1007/BF02798541

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