Coenzyme production using immobilized enzymes. III. Immobilization of glucose-6-phosphate dehydrogenase from Bakers' yeast

M. Kotorman, L. M. Simon, B. Szajani

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7 Citations (Scopus)

Abstract

Glucose-6-phosphate dehydrogenase (d-glucose-6-phosphate: NADP+ 1-oxidoreductase, EC 1.1.1.49) from Bakers' yeast was immobilized with the highest activity on polyacrylamide beads possessing carboxylic functional groups activated by a water-soluble carbodiimide. The optimal pH values for the catalytic activity of the soluble and the immobilized glucose-6-phosphate dehydrogenase were practically identical, lying between pH 9.0 and 9.2. The optimal temperature for both the soluble and the immobilized enzyme was about 50°C. The apparent Km values of the immobilized enzyme were slightly higher than those of the soluble enzyme. The immobilization improved the stability of the enzyme in the pH range 6.0-9.0 at 45°C. The operational stability of the immobilized glucose-6-phosphate dehydrogenase proved favorable in a column experiment during 37 days of opeartion.

Original languageEnglish
Pages (from-to)974-978
Number of pages5
JournalEnzyme and Microbial Technology
Volume16
Issue number11
DOIs
Publication statusPublished - Nov 1994

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Keywords

  • NADP
  • NADPH
  • continuous production
  • glucose-6-phosphate dehydrogenase
  • immobilized

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Biochemistry
  • Applied Microbiology and Biotechnology

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