Invert Sugar Production Research Articles

Immobilization of invertase within calcium alginate gel capsules

Saccharomyces cerevisiae invertase was immobilized in alginate capsules. The immobilization resulted in 87% relative activity and activity for 36 days without decrease in activity. Optimum conditions for activity were not affected by immobilization and the optimum pH and temperature for free and immobilized enzyme were 4.3 and 60°C, respectively. Immobilized invertase was however, more stable at high pH and temperatures. The kinetic parameters for free and immobilized invertase were also determined. Since the process is simple and invertase does not leak out of capsules, this method can be used for the industrial production of invert sugar.

Studies on Sugar-isomerizing Enzyme

A glucose isomerase which reversibly catalyzes the reaction between d-glucose and d-fructose was demonstrated in the cell-free extracts of a strain of Streptomyces sp. isolated from soil. The enzyme was produced when the strain was grown in the medium containing xylan or xylan-containing material such as wheat bran. A medium which consists of 3% of wheat bran, 2% of corn steep liquor and 0.024% of CoCl2·6H2O is recommendabie for the production of the glucose isomerase enzyme with the strain. With the enzyme, some conditions for the conversion of d-glucose to d-fructose were also studied. The method is very useful for the production of invert sugar from d-glucose and is now on the way to be applied to the practical use.