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Relevant bibliographies by topics / P-nitrophenyl-β-D-glucoside

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Academic literature on the topic 'P-nitrophenyl-β-D-glucoside'

Author: Grafiati

Published: 5 June 2025

Last updated: 2 August 2025

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Journal articles on the topic "P-nitrophenyl-β-D-glucoside"

1

OPASSIRI, Rodjana, Yanling HUA, Onnop WARA-ASWAPATI, et al. "beta-Glucosidase, exo-beta-glucanase and pyridoxine transglucosylase activities of rice BGlu1." Biochemical Journal 379, no. 1 (2004): 125–31. http://dx.doi.org/10.1042/bj20031485.

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The bglu1 cDNA for a β-glucosidase cloned from rice (Oryza sativa L.) seedlings was expressed as a soluble and active protein in Escherichia coli and designated BGlu1. This enzyme hydrolysed β-1,4-linked oligosaccharides with increasing catalytic efficiency (kcat/Km) values as the DP (degree of polymerization) increased from 2 to 6. In contrast, hydrolysis of β-1,3-linked oligosaccharides decreased from DP 2 to 3, and polymers with a DP greater than 3 were not hydrolysed. The enzyme also hydrolysed p-nitrophenyl β-d-glycosides and some natural glucosides but with lower catalytic efficiency tha

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2

Bhat, M. K. "Potential application of cellulase and hemicellulase assay techniques for assessing the forage quality and performance of rumen micro-organisms." BSAP Occasional Publication 22 (1998): 290–93. http://dx.doi.org/10.1017/s0263967x00032900.

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Cellulose and hemicellulose are the major structural polysaccharides of plant cell wall. The efficient utilization of these polysaccharides by ruminants is often restricted by the presence of lignin. Cellulose and hemicellulose are hydrolysed by a group of enzymes called cellulases and hemicellulases. The present paper describes the cellulase and hemicellulase assay methods and their potential applications.Carboxymethyl (CM)-cellulose, Avicel, cellobiose, xylobiose, p-nitrophenyl-p β-D-glucoside (pNPG), p-nitrophenyl-β-D-cellobioside (pNPC), p-nitrophenyl-β-D-xyloside (pNPX) and p-nitrophenyl-

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3

Shlini, Purushothaman, та Murthy K. R. Siddalinga. "Extraction of β-galactosidase and β-glucosidase from the seeds of Tamarindus indica". International Journal of Biomolecules and Biomedicine (IJBB) 1, № 3 (2011): 8–17. https://doi.org/10.5281/zenodo.8285181.

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The enzymes β–galactosidase and β–glucosidase were extracted from the tamarind seeds using different buffers at different pH. Highest activity was obtained with 10 mM sodium acetate buffer, pH 5.6 and 10 mM tris buffer, pH 7.4. The effect of NaCl and Triton X–100 at different concentrations on the extraction of the enzymes indicated 10 mM sodium acetate buffer, pH 5.6 containing 1 M NaCl as a better extractant of the enzyme. The enzyme assay was carried out using p–nitrophenyl–β–D–galactoside and p–nitrophenyl–β–D&

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4

Cohen-Forterre, L., A. M. Grigorova-Borsos, C. Falcy, et al. "Alteration in sialidase and other glycosidase activities in the kidney of spontaneously hypertensive rats: persistence after preventive treatment with hydralazine." Canadian Journal of Physiology and Pharmacology 66, no. 7 (1988): 884–88. http://dx.doi.org/10.1139/y88-144.

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Because kidney microangiopathy with capillary basement membrane thickening has been reported in spontaneous hypertension, we have studied the activities of three lysosomal glycosidases able to degrade the carbohydrate moieties of basement membrane constituents in the kidney cortex of 12-week-old spontaneously hypertensive rats (SHR) and age-matched normotensive Wistar Kyoto rats (WKY). These activities were also determined in SHR and WKY treated from 6 to 12 weeks of age with hydralazine (mean dose, 18 mg/kg per day in drinking water). Sialidase specific activity on sialyl-α2-3-[3H]lactitol wa

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5

Fogarty, William M., Catherine T. Kelly та Sunil K. Kadam. "Separation and characterization of an α-glucosidase and maltase from Bacillus amyloliquefaciens". Canadian Journal of Microbiology 31, № 8 (1985): 670–74. http://dx.doi.org/10.1139/m85-127.

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A novel α-glucosidase and a maltase were isolated from Bacillus amyloliquefaciens. The formation of both enzymes was induced by trehalose, sucrose, or lactose in the growth medium. Trehalose is by far the most efficient inducer of both systems. The α-glucosidase and maltase were separated and purified by ion-exchange chromatography on DEAE Bio-Gel A. Purified α-glucosidase hydrolysed p-nitrophenyl-α-D-glucoside, isomaltose, and isomaltotriose but sucrose, maltose, or related saccharides were not attacked. β-Glucosides and polymeric glucosides were not degraded. The optimum temperature for α-gl

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6

Mei, Jianfeng, Xia Wu, Sujing Zheng, Xiang Chen, Zhuliang Huang та Yichun Wu. "Improvement of Cucurbitacin B Content in Cucumis melo Pedicel Extracts by Biotransformation Using Recombinant β-Glucosidase". Separations 8, № 9 (2021): 138. http://dx.doi.org/10.3390/separations8090138.

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For the efficient biotransformation of cucurbitacin B 2-o-β-d-glucoside (CuBg) to cucurbitacin B (CuB) in Cucumis melo pedicel extracts, the β-glucosidase gene bglS—consisting of 1344 bp (447 amino acids) from Streptomyces sp. RW-2—was cloned and expressed in Escherichia coli BL21(DE3). The activity of recombinant β-glucosidase with p-nitrophenyl-β-d-glucoside (pNPG) as a substrate was 3.48 U/mL in a culture. Using the recombinant β-glucosidase for the biotransformation of C. melo pedicel extracts, CuBg was converted into CuB with a conversion rate of 87.6% when the concentration of CuBg was 0

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7

Lin, Johnson, Balakrishna Pillay та Suren Singh. "Purification and biochemical characteristics of β‐D‐glucosidase from a thermophilic fungus, Thermomyces lanuginosus–SSBP". Biotechnology and Applied Biochemistry 30, № 1 (1999): 81–87. http://dx.doi.org/10.1111/j.1470-8744.1999.tb01163.x.

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The β‐D‐glucosidase produced by Thermomyces lanuginosus‐SSBP was purified to apparent homogeneity. The purified enzyme consisted of two identical subunits with a native molecular mass of 200 kDa. The purified β‐D‐glucosidase only hydrolysed the glucoside substrates containing a terminal, non‐reducing β‐D‐glucose residue and was active on both aryl‐β‐glucoside and cellobiose. This enzyme also exhibited less, but significant α‐D‐glucosidase activity and was capable of hydrolysing β‐1,6‐linked diglucosides and gentiobiose. The K appm, Vmax and kcat values for p‐nitrophenyl‐β‐D‐glucopyranoside wer

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8

KERESZTESSY, Zsolt, Jane HUGHES, László KISS та Monica A. HUGHES. "Co-purification from Escherichia coli of a plant β-glucosidase-glutathione S-transferase fusion protein and the bacterial chaperonin GroEL". Biochemical Journal 314, № 1 (1996): 41–47. http://dx.doi.org/10.1042/bj3140041.

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The coding sequence of the mature cyanogenic β-D-glucosidase (β-D-glucoside glucohydrolase, EC 3.2.1.21) (linamarase) of Manihot esculenta Crantz (cassava) was cloned into the vector pGEX-2T and expressed in Escherichia coli. The bacterial chaperonin GroEL [Braig, Otwinowski, Hedge, Boisvert, Joachimiak, Horwich and Sigler (1994) Nature (London) 371, 578–586] was found to be tightly associated with the fusion protein and co-purified with it. In the presence of excess MgATP, release and folding of the fusion β-glucosidase were demonstrated by a fast increase in both linamarase and p-nitrophenyl

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9

Tan, Larry U. L., Paul Mayers, Michelle Illing та John N. Saddler. "The copurification of β-glucosidase, β-xylosidase, and 1,3-β-glucanase in two separate enzyme complexes isolated from Trichoderma harzianum E58". Biochemistry and Cell Biology 65, № 9 (1987): 822–32. http://dx.doi.org/10.1139/o87-107.

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Two enzyme complexes, each with β-glucosidase (β-D-glucoside glucohydrolase, EC 3.2.1.21), β-xylosidase (β-D-xylan xylohydrolase, EC 3.2.1.37), and 1,3-β-glucanase (laminarinase, EC 3.2.1.39) activity, were purified to near homogeneity from the cellulolytic fungus Trichoderma harzianum E58. The two complexes had the same isoelectric point of pH 8.3 and identical subunit molecular masses of 75 400 daltons. The two complexes were also similar in that all activities were sensitive to inhibition by mercuric chloride (2 mM) and D-glucono-1,5-lactone (0.2% w/v). The activity ratios of the major and

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10

Riou, Christine, Jean-Michel Salmon, Marie-Jose Vallier, Ziya Günata та Pierre Barre. "Purification, Characterization, and Substrate Specificity of a Novel Highly Glucose-Tolerant β-Glucosidase fromAspergillus oryzae". Applied and Environmental Microbiology 64, № 10 (1998): 3607–14. http://dx.doi.org/10.1128/aem.64.10.3607-3614.1998.

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ABSTRACT Aspergillus oryzae was found to secrete two distinct β-glucosidases when it was grown in liquid culture on various substrates. The major form had a molecular mass of 130 kDa and was highly inhibited by glucose. The minor form, which was induced most effectively on quercetin (3,3′,4′,5,7-pentahydroxyflavone)-rich medium, represented no more than 18% of total β-glucosidase activity but exhibited a high tolerance to glucose inhibition. This highly glucose-tolerant β-glucosidase (designated HGT-BG) was purified to homogeneity by ammonium sulfate precipitation, gel filtration, and anion-ex

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