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Applied Biochemistry and Biotechnology

, Volume 36, Issue 1, pp 1–12 | Cite as

Immobilized triosephosphate isomerases a comparative study

  • Magdolna Áabrahám
  • A. Alexin
  • B. Szajáni
Article
  • 32 Downloads

Abstract

Pig muscle triosephosphate isomerase was covalently attached to polyacrylamide and silica-based supports possessing carboxylic or aldehyde functional groups or activated with p-benzoquinone. A silica-based support activated with p-benzoquinone proved to be the most advantageous. There were no profound alterations in the catalytic properties as a result of the immobilization. The immobilization enhanced the resistance against urea and heat treatment. At the start of the treatments, the enzyme was activated. The extent of activation depended on the pH, and on the buffer and salt concentrations. Increase of the ionic strength decreased or eliminated the activation. The phosphate ion had a specific effect on the thermal inactivation.

Index Entries

Triosephosphate isomerase, immobilized support, silica-based support, polyacrylamide-type catalytic properties, immobilized triosephosphate isomerase stability tests, immobilized triosephosphate isomerase 

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Copyright information

© Humana Press Inc. 1992

Authors and Affiliations

  • Magdolna Áabrahám
    • 1
  • A. Alexin
    • 2
  • B. Szajáni
    • 2
  1. 1.Department of BiochemistryAtilla József UniversitySzeged, 6701Hungary
  2. 2.Reanal Factory of Laboratory ChemicalsBudapest 70Hungary

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