| Abstract: | Transglucosyl-amylase was purified 96-fold and partially characterized. The K(m) value with dextrin as substrate was 9.1 mg/ml. Glycerol, an acceptor of d-glucose, appeared to inhibit dextrin hydrolysis noncompetitively. The energy of activation of the enzyme was 7,920 cal/mole. Indirect determinations showed that synthesis of d-glucosyl glycerol was significantly affected by the nature of the amylaceous substrate. Glucosyl-glycerol synthesis did not increase as incubation temperature was raised from 50 to 60 C. Direct determinations by gas-liquid chromatography indicated that the synthesis of glucosyl glycerol, as a function of the concentration of either enzyme, substrate, or glycerol, traced a curvilinear path approaching 15 mg/ml as the maximum. When enzyme, substrate, and glycerol at high concentrations were varied in all possible combinations, however, conditions for producing as much as 47.5 mg/ml of glucosyl glycerol were established. |
