Glucose Isomerase Activity

Table VI. Effect of Diethylpyrocarbonate (DEPC) on Thermoanaerobe Glucose Isomerase Activity of the Wild-Type and Mutant Enzymes ...

Note Glucose isomerase activity of the commercial enzyme is usually determined on the enzyme that has been immobilized by binding with a polymer matrix or other suitable material. The following method is designed for use with such preparations. 

Amyloglucosidase Activity), 798 Glucose Isomerase Activity, 796 Glucose Oxidase Activity, 798 P-D-Glucosidase Activity, 798 Hemicellulase Activity, 799 Invertase Activity, 800 Lactase (Acid) (P-Galactosidase) Activity, 802... 

The conversion of D-glucose (17) into D-fructose (9) by a microbial enzyme (Scheme 5) was first reported in 1957 when Marshall and Kooi found glucose isomerase activity in cell-free extracts of Pseudomonas hydrophila (91. This enzymatic activity was enhanced in the presence of arsenate. Soon thereafter, other arsenate-requiring enzymes were isolated from Aerobacter sp. as well as Escherichia freundii [10]. Enzymes required arsenate when D-glucose or D-fructose was the substrate but not when the corresponding 6-phosphates 11 and 12 were offered. Purification of the arsenate-dependent principle component from Escherichia intermedia allowed the conclusion that the enzyme was a glucose 6-phosphate isomerase (EC 5.3.1.9) that was able to isomerise free D-glucose when it was complexed with arsenate [11]. 

D-Glucose Isomerases.—Active immobilized forms of D-glucose isomerase have been obtained by reaction with cyanogen bromide-treated alumina, glass, or titania. ... 

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