P-D-glucosidase activity

Figure 9. Enzyme production by T. reesei QM 9414 incubated in the presence of ImM sophorose. The incubation medium (27) included 17mM potassium phosphate buffer, pH 6.0, at 28°C. The appearance of aryl-p-D-glucosidase activity (A) in the extracellular medium is delayed in comparison to endoglucanase activity (O) and Avicelase activity ( ).

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... 

Quiquampoix H (1987) A stepwise approach to the understanding of extracellular enzyme activity in soil. I. Effect of electrostatic interactions on the conformation of a P-D-glucosidase adsorbed on different mineral surfaces. Biochimie 69 753-763... 

T. Granier, N. Panday, and A. Vasella, Structure-activity relations of imidazo-pyridine-type inhibitors of P-D-glucosidases, Helv. Chim. Acta, 80 (1997) 979-987. 

Our group has demonstrated that the catalytic properties of immobilized enzymes can be manipulated by the temperature-dependent swelling behavior of the microgel. The hydrolytic activity of adsorbed and native P-D-glucosidase was determined as a function of temperature. Desorption of immobilized enzyme upon... 

Fig. 19 Reactions used for testing the activity of enzymes (P-D-glucosidase) immobilized in the thermo sensitive core-shell microgel template at different temperatures. Enzymatic hydrolysis of the substrate oNPG produces d-glucose and o-nitrophenol. The concentration of the resulting o-nitrophenol can be monitored photometrically...

Thus, the results shown here demonstrate that thermosensitive microgel particles can serve as superior carriers for the adsorption of enzymes in which the activity of adsorbed enzymes are preserved. The catalytic activity of adsorbed P-D-glucosidase from almonds is increased by a factor of more than three. Moreover, the catalytic properties of immobilized enzymes can be manipulated by the volume transition of the microgel. Hence, such microgels present a novel class of active nanoreactors for biocatalysis. 

Manzanares, P, Rojas, V., Genoves, S., Valles, S. (2000) A preliminary search for anthocyanin-beta-D-glucosidase activity in non-Saccharomyces wine yeasts. International Journal of Food Science and Technology, 35, 95-103. 

Scholz, O. and Boon, P.l. (1993) Alkaline phosphatase, aminopeptidase and (5-D glucosidase activities associated with billabong periphyton. Archiv fur Hydrobiologie 125, 429 43. 

Ghosh P, Pamment NB, Martin WRB. (1982). Simultaneous saccharification and fermentation of cellulose—effect of beta-d-glucosidase activity and ethanol inhibition of ceUulases. Enzyme Microb Technol, 4(6), 425 30. 

An increase in the level of amylase activity was observed on hybridization of a hyperderepressed strain of Neurospora crassa with the normal strain. Both a- and P-D-glucosidases have been detected in axenic cultures of the myxomycete Physarum polycephalum. ... 

An active immobilized form of a-D-glucosidase has been obtained by reaction of the enzyme with agarose cyclic imidocarbonate. Active immobilized forms of P-D-glucosidase have been prepared by chelation of the enzyme with hydrous oxides of iron(iii), tin(ii), vanadium(iii), and zirconium(iv), and by reaction of the enzyme with diazotized 1,4-diaminobenzene and with agarose cyclic imidocarbonate. ... 

The fungus Papulaspora thermophila has been shown to degrade filter paper and soluble carboxymethylcellulose. Synthesis of the cellulolytic enzymes could be induced by cellulosic material added to the growth medium. A cytosolic P-D-glucosidase from Pseudomonas fluorescens possesses some exo-cellulase activity. " " ... 

During a study of the properties of two j8-D-galactosidases from human liver, it emerged that the isoenzymes also possessed /S-D-glucosidase activity (pH optima 6.2) (see p. 394). ... 

Cellobiose or cellulose were necessary to induce the production of fS-D-glucosidase activity by Sporotrichum pulverulentum. Purification via preparative slab gel isoelectric focusing and affinity chromatography on a phenyl derivative of agarose gave five active fractions (p/ s 4.5—5.2, mol. wts. 1.65—1.82 X 10 by sodium dodecyl sulphate-polyacrylamide gel electrophoresis). 

P-D-Glucosidases.— The active site of the jS-D-glucosidase from Aspergillus wentii has been labelled by reaction with the epoxide of [ H]conduritol The derivative was used in sequence studies of the enzyme. A reduced and alkylated derivative of the ) -D-glucosidase from crude Trichoderma viride cellulase has been prepared. ... 

The -D-glucosidase activities of several plants Arachis hypogaea, Cicer arietinum, Phaseolus mango, and P. radiatus) were inhibited by D-xylose. ... 

In order to account for the inability of many enzymes to bind the protonated form of the basic inhibitors or permanently cationic ones better than uncharged analogs (for example, yS-o-galactosidase from E. coli, and P-v>-glucosidase from almonds), it was proposed that the enzyme could proton-ate the inhibitor at the active site by a cationic acid (for example, protonated histidine). If proton transfer cannot occur, the attractive forces due to the carboxylate would be canceled by the repulsion from the cationic acid. Experimental evidence for this proposal is, however, still lacking. In fi-D-gn-lactosidase from E. coli, a tyrosine is presumed to be responsible for the protonation of substrates. ... 

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