Glucose-6-phosphate dehydrogenase (d-glucose-6-phosphate: NADP+ 1-oxidoreductase, EC 188.8.131.52) 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.
- continuous production
- glucose-6-phosphate dehydrogenase
ASJC Scopus subject areas
- Applied Microbiology and Biotechnology