Comparative studies on soluble and immobilized yeast hexokinase

L. M. Simon, M. Nagy, M. Ábrahám, B. Szajáni, L. Boross

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

Comparative studies have been carried out on soluble and immobilized yeast hexokinase (ATP: D-hexose 6-phosphotransferase, EC 2.7.1.1). The enzyme was immobilized by covalent attachment to a polyacrylamide type support containing carboxylic functional groups. The effects of immobilization on the catalytic properties and stability of hexokinase were studied. As a result of immobilization, the pH optimum for catalytic activity was shifted in the alkaline direction to ∼pH 9.7. The apparent optimum temperature of the immobilized enzyme was higher than that of the soluble enzyme. The apparent Km value with D-glucose as substrate increased, while that with ATP as substrate decreased, compared with the data for the soluble enzyme. Differences were found in the thermal inactivation processes and stabilities of the soluble and immobilized enzymes. The resistance to urea of the soluble enzyme was higher at alkaline pH values, while that for the immobilized enzyme was greatest at ∼pH 6.0.

Original languageEnglish
Pages (from-to)275-278
Number of pages4
JournalEnzyme and Microbial Technology
Volume7
Issue number6
DOIs
Publication statusPublished - Jun 1985

Keywords

  • Yeast
  • catalytic properties
  • covalent coupling
  • immobilization of hexokinase
  • stability
  • yeast hexokinase

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Biochemistry
  • Applied Microbiology and Biotechnology

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