Catalytic efficiency of immobilized glucose isomerase in isomerization of glucose to fructose

Glucose isomerase (GI) from Streptomyces rubiginosus was immobilized covalently onto Eupergit C 250 L made by copolymerization of N,N-methylene-bis-methacrylamide, glycidyl methacrylate, allyl glycidyl ether and methacrylamide. The catalytic efficiency of immobilized GI in isomerization of glucose to fructose was found as three fold higher than that of free GI. The residual activity of immobilized GI after 18 reuses in a batch type stirred reactor was about 85% of its initial activity. The thermal stability of immobilized GI was almost same with that of the free GI at 60 °C for 18 h preincubation time. The residual activities of immobilized GI when stored at 5 °C and 25 °C for four weeks were 72% and 69% of the initial activity, respectively. However, free GI retained 88% and 78% of its initial activity at 5 °C and 25 °C upon four weeks storage, respectively. Thus, the use of Eupergit C 250 L immobilized GI instead of free GI is suggested in enzymatic isomerization of glucose to fructose.