Applied Biochemistry and Biotechnology

, Volume 11, Issue 2, pp 91–100 | Cite as

Characterization and comparison of soluble and immobilized pig muscle aldolases

  • Magdolna Ábrahám
  • Lóránt Horvth
  • Mária Simon
  • Béla Szajńi
  • Lászl Boross
Original Articles


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.

Index Entries

Immobilized aldolase pig muscle aldolase covalent attachment polyacrylamide matrix, containing carboxylic functional groups Akrilex C-100 gel, with high aldolase activity aldolase, with high stability 


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Copyright information

© The Humana Press Inc 1985

Authors and Affiliations

  • Magdolna Ábrahám
    • 1
  • Lóránt Horvth
    • 1
  • Mária Simon
    • 1
  • Béla Szajńi
    • 1
  • Lászl Boross
    • 1
  1. 1.Department of BiochemistryAttila József UniversityKözépfasorHungary

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