P-D-Glucosidase

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... 

D. E. Walker and B. Axelrod, Evidence for a single catalytic site on the P-d-glucosidase-P-D-galactosidase of almond emulsin, Arch. Biochem. Biophys., 187 (1978) 102-107. 

B. W. Sigurdskjold, B. Duus, and K. Bock, Hydrolysis of substrate analogues catalysed by P-D-glucosidase from Aspergillus niger. Part II Deoxy and deoxyhalo derivatives of cellobiose, Acta Chem. Scand., 45 (1991) 1032-1041. 

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. 

G. M. Aerts, O. Van Opstal, and C. K. De Bruyne, Mixed inhibition of P-D-glucosidase from Stachybotrys atra by substrate analogues, Carbohydr. Res., 138 (1985) 127-134. 

N. Baggett, M. A. Case, P. R. Darby, and C. J. Cray, Action of almond P-D-glucosidase on fluorogenic substrates derived from 4-substituted 7-hydroxycoumarins, Enzyme Microb. Technol., 15 (1993) 742-748. 

Le Traon-Masson, M.-P. and Pellerin, P., Purification and characterization of two P-D-glucosidases from an Aspergillus niger enzyme preparation affinity and specificity toward glucosylated compounds characteristic of the processing of fruits. Enzyme Microb. Technol 22, 374, 1998. 

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 ( ).

GEERLINGS, A., MARTINEZ-LOZANO IBANEZ, M., MEMELINK, J., VAN DER HEIJDEN, R., VERPOORT, R., Molecular cloning and analysis of strictosidine P-D-glucosidase, an enzyme in terpenoid indole alkaloid biosynthesis in Catharanthus roseus. J. Biol. Chem., 2000,275,3051-3056. 

The versatility of strictosidine as a central intermediate for the biosynthesis of a variety of alkaloids is based on the highly reactive dialdehyde produced by the action of strictosidine p-D-glucosidase. This reactive intermediate is converted by uncharacterized enzymes into the major corynanthe, iboga, and aspidosperma skeletons that are elaborated into die several hundred alkaloids found in Catharanthns roseus. Since the biosynthesis of strictosidine appears to occur within plant vacuoles, there has been much speculation, but little is known, about the factors that regulate the accumulation of strictosidine within the vacuole, or which trigger its mobilization for further elaboration. It is well known that glycosides of different natural product classes are located within plant vacuoles. 

P-D-Glucosidase Hydrolysis of terminal, nonreducing (3-D-glucose residues with the release of (3-D-glucose. 

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... 

Fig. 16 The adsorbed amount of P-d-glucosidase per gram microgel Ta(js is plotted versus the concentration of free enzyme csoi in solution. The dashed line represents the fit of the experimental data by (2). The arrow marks the amount of entrapped enzyme used for kinetic investigation (620 mg P-D-glucosidase per gram microgel). The inset displays the data as a linear Langmuir plot. The adsorption was conducted at 4°C in 10 mM MOPS buffer solution (pH 7.2) and with a micro-gel concentration of 1 wt%. The immobilized enzymes do not prevent the microgel from shrinking at temperatures above the LCST [23]...

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...

Table 3 Kinetic parameters of native and immobilized P-D-glucosidase at 20°C and 40°C [23] ...

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. 

N-acetylglucosamine to oligosaccharides Endohydrolysis of 1,4-p-D-glucosidic linkages in cehulose 1,4-p-D-glucosidase... 

Shulman, M L, Shiyan, S D, Khorhn, A Y, The s3mthesis of diasteromeric epoxy-(P-D-glucopyranosyl)ethanes and l,2-epoxy-3-(P-D-glucopyranosyl)propanes, as irreversible inhibitors of p-D-glucosidase, Carbohydr. Res., 33, 229-235, 1974. 

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