Glucose oxidase 1-Glucosidase

A liquid membrane bioreactor was developed as a means of encapsulation for a multi-enzyme system incorporating an oxidation and carbohydrate cleavage, demonstrated using a-glucosidase and glucose oxidase in the conversion of maltose to gluconic acid ... 

The protein content of honey is usually around 0.2% (Anklam, 1998 Iurlina and Fritz, 2005). A small portion of this fraction consists of enzymes, notably invertase, diastase, amylase, glucose oxidase, catalase (Anklam, 1998), a-glucosidase, and p-glucosidase (Won et al., 2008). Some are derived from bees, whereas others come from the nectar. Enzyme activity varies among honey samples since the amount of bee saliva, the source of bee enzymes, found in honey varies with the conditions of honey production (Anklam, 1998). 

Fig. 6. Temperature dependency of activity yield in the immobilization of enzymes by radiation polymerization. Enzyme O ot-amylase in 50% HEMA A glucoamyla.se in 50% HEMA cellulase in 50% HEMA glucose oxidase in 50% HEMA A glucoamylase in 30% HEMA a-glucosidase in 50% HEMA. Monomer HEMA (2-hydroxyethyl methacrylate). Irradiation. 1 x 106 rad, in vacuo. % monomen in buffer solution...

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... 

Figure 6. Both hydrolytic and oxidative enzymes participate in cellulose decomposition by the white-rot fungus Phanerochaete chrysosporium Burds. Hydrolytic enzymes i, endo-1 - - I ucanases 2, exo-1,4- -glucanase and 3, -glucosidase. Oxidative enzymes 4, glucose oxidase, 5, cMlobiose oxidise and 6, cellobiose quinone oxidoreductase. Adapted from Reference 23,...

Prepared from coniferin with glucosidase, glucose oxidase, and peroxidase at pH 5. 

While this paper deals with the chemistry and reaction characteristics of glucose isomerase, it should be noted that glucose oxidase, glucoamylase, aldose-1-epimerase, a-glucosidase, alcohol dehydrogenase, pullulanase, and fungal a-amylase have been successfully immobilized onto this support. 

Infrared spectroscopic studies of glucose oxidase (Parker, 1962a), invertase (Parker, 1962fc), and )S-glucosidase (Parker, 1964) in aqueous solutions have been reported. In the case of the latter two enzymes, kinetic studies were done (see also, Parker, 1967). The substrate used with )S-glucosidase was phenyl )S-D-glucoside. Rate constants were calculated from absorbance data of the free-glucose band at 1149 cm . 

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