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

Author: Grafiati

Published: 5 June 2025

Last updated: 2 August 2025

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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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11

PARRY, Neil J., David E. BEEVER, Emyr OWEN, Isabel VANDENBERGHE, Jozef VAN BEEUMEN та Mahalingeshwara K. BHAT. "Biochemical characterization and mechanism of action of a thermostable β-glucosidase purified from Thermoascus aurantiacus". Biochemical Journal 353, № 1 (2000): 117–27. http://dx.doi.org/10.1042/bj3530117.

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An extracellular β-glucosidase from Thermoascus aurantiacus was purified to homogeneity by DEAE-Sepharose, Ultrogel AcA 44 and Mono-P column chromatography. The enzyme was a homotrimer, with a monomer molecular mass of 120kDa; only the trimer was optimally active at 80°C and at pH 4.5. At 90°C, the enzyme showed 70% of its optimal activity. It was stable at pH 5.2 and at temperatures up to 70°C for 48h, but stability decreased above 70°C and at pH values above and below 5.0. The enzyme hydrolysed aryl and alkyl β-d-glucosides and cello-oligosaccharides, and was specific for substrates with a β

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12

Opassiri, Rodjana, Busarakum Pomthong, Takashi Akiyama та ін. "A stress-induced rice (Oryza sativa L.) β-glucosidase represents a new subfamily of glycosyl hydrolase family 5 containing a fascin-like domain". Biochemical Journal 408, № 2 (2007): 241–49. http://dx.doi.org/10.1042/bj20070734.

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GH5BG, the cDNA for a stress-induced GH5 (glycosyl hydrolase family 5) β-glucosidase, was cloned from rice (Oryza sativa L.) seedlings. The GH5BG cDNA encodes a 510-amino-acid precursor protein that comprises 19 amino acids of prepeptide and 491 amino acids of mature protein. The protein was predicted to be extracellular. The mature protein is a member of a plant-specific subgroup of the GH5 exoglucanase subfamily that contains two major domains, a β-1,3-exoglucanase-like domain and a fascin-like domain that is not commonly found in plant enzymes. The GH5BG mRNA is highly expressed in the shoo

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13

Sørensen, Annette, Birgitte K. Ahring, Mette Lübeck та ін. "Identifying and characterizing the most significant β-glucosidase of the novel species Aspergillus saccharolyticus". Canadian Journal of Microbiology 58, № 9 (2012): 1035–46. http://dx.doi.org/10.1139/w2012-076.

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The newly discovered fungal species Aspergillus saccharolyticus was found to produce a culture broth rich in β-glucosidase activity. In this present work, the main β-glucosidase of A. saccharolyticus responsible for the efficient hydrolytic activity was identified, isolated, and characterized. Ion exchange chromatography was used to fractionate the culture broth, yielding fractions with high β-glucosidase activity and only 1 visible band on an SDS–PAGE gel. Mass spectrometry analysis of this band gave peptide matches to β-glucosidases from aspergilli. Through a polymerase chain reaction approa

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14

Thompson, John, Sergei B. Ruvinov, Darón I. Freedberg, and Barry G. Hall. "Cellobiose-6-Phosphate Hydrolase (CelF) ofEscherichia coli: Characterization and Assignment to the Unusual Family 4 of Glycosylhydrolases." Journal of Bacteriology 181, no. 23 (1999): 7339–45. http://dx.doi.org/10.1128/jb.181.23.7339-7345.1999.

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ABSTRACT The gene celF of the cryptic cel operon ofEscherichia coli has been cloned, and the encoded 6-phospho-β-glucosidase (cellobiose-6-phosphate [6P] hydrolase; CelF [EC 3.2.1.86 ]) has been expressed and purified in a catalytically active state. Among phospho-β-glycosidases, CelF exhibits unique requirements for a divalent metal ion and NAD+ for activity and, by sequence alignment, is assigned to family 4 of the glycosylhydrolase superfamily. CelF hydrolyzed a variety of P-β-glucosides, including cellobiose-6P, salicin-6P, arbutin-6P, gentiobiose-6P, methyl-β-glucoside-6P, and the chromog

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15

KERESZTESSY, Zsolt, Kate BROWN, M. Alison DUNN та Monica A. HUGHES. "Identification of essential active-site residues in the cyanogenic β-glucosidase (linamarase) from cassava (Manihot esculenta Crantz) by site-directed mutagenesis". Biochemical Journal 353, № 2 (2001): 199–205. http://dx.doi.org/10.1042/bj3530199.

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The coding sequence of the mature cyanogenic β-glucosidase (β-glucoside glucohydrolase, EC 3.2.1.21; linamarase) was cloned into the vector pYX243 modified to contain the SUC2 yeast secretion signal sequence and expressed in Saccharomyces cerevisiae. The recombinant enzyme is active, glycosylated and showed similar stability to the plant protein. Michaelis constants for hydrolysis of the natural substrate, linamarin (Km = 1.06mM) and the synthetic p-nitrophenyl β-D-glucopyranoside (PNP-Glc; Km = 0.36mM), as well as apparent pKa values of the free enzyme and the enzymeŐsubstrate complexes (pKE1

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16

Huang, Meng, Salila Pengthaisong, Ratana Charoenwattanasatien, Natechanok Thinkumrob, Jitrayut Jitonnom, and James R. Ketudat Cairns. "Systematic Functional and Computational Analysis of Glucose-Binding Residues in Glycoside Hydrolase Family GH116." Catalysts 12, no. 3 (2022): 343. http://dx.doi.org/10.3390/catal12030343.

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Glycoside hydrolases (GH) bind tightly to the sugar moiety at the glycosidic bond being hydrolyzed to stabilize its transition state conformation. We endeavored to assess the importance of glucose-binding residues in GH family 116 (GH116) β-glucosidases, which include human β-glucosylceramidase 2 (GBA2), by mutagenesis followed by kinetic characterization, X-ray crystallography, and ONIOM calculations on Thermoanaerobacterium xylanolyticum TxGH116, the structural model for GH116 enzymes. Mutations of residues that bind at the glucose C3OH and C4OH caused 27–196-fold increases in KM for p-nitro

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17

Zhou, Zhen Zhen, та Yu Qing Zhang. "Biosynthesis of β-Glucosidase-Silk Fibroin Nanoparticles Conjugates and Enzymatic Characteristics". Advanced Materials Research 175-176 (січень 2011): 186–91. http://dx.doi.org/10.4028/www.scientific.net/amr.175-176.186.

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Silk fibroin derived from Bombyx mori is a biomacromolecular protein with outstanding biocompatibility. When it was dissolved in highly concentrated CaCl2 solution and then the mixture of the protein and salt was subjected to desalting treatments for long time in flowing water, the resulting liquid silk was water-soluble polypeptides with different molecular masses, ranging from 10 to 200 kDa. When the liquid silk were introduced rapidly into acetone, silk protein nanoparticles (SFNs) with a range of 40~120 nm in diameter could be obtained. The crystalline silk nanoparticles could be conjugate

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18

Umezurike, G. M. "The effect of glycerol on the activity of β-glucosidase from Botryodiplodia theobromae Pat". Biochemical Journal 254, № 1 (1988): 73–76. http://dx.doi.org/10.1042/bj2540073.

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1. In the activity of the high-Mr beta-glucosidase A (beta-D-glucoside glucohydrolase, EC 3.2.1.21) obtained from culture filtrates of Botryodiplodia theobromae Pat. on o-nitrophenyl beta-D-glucopyranoside as substrate, both Vmax. and Km increased non-linearly with increasing concentration of glycerol, and the Vmax./Km(app.) ratio decreased non-linearly with increasing concentration of glycerol. 2. No increase in rate was observed with phenyl beta-D-glucopyranoside as substrate in the presence of up to 250 mM-glycerol, indicating that glucosylation is rate-limiting with this substrate. 3. With

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19

LaMarco, K. L., та R. H. Glew. "Hydrolysis of a naturally occurring β-glucoside by a broad-specificity β-glucosidase from liver". Biochemical Journal 237, № 2 (1986): 469–76. http://dx.doi.org/10.1042/bj2370469.

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We have isolated from guinea-pig liver a broad-specificity beta-glucosidase of unknown function that utilizes as its substrate non-physiological aryl glycosides (e.g. 4-methylumbelliferyl beta-D-glucopyranoside, p-nitrophenyl beta-D-glucopyranoside). The present paper documents that this enzyme can be inhibited by various naturally occurring glycosides, including L-picein, dhurrin and glucocheirolin. In addition, L-picein, which acts as a competitive inhibitor of the broad-specificity beta-glucosidase (Ki 0.65 mM), is also a substrate for this enzyme (Km 0.63 mM; Vmax. 277,000 units/mg). Heat-

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20

Ibrahim, Salah M., and Abbas S. Al-Mizraqchi. "Comparison of the Antibacterial Activity of Panax Ginseng and Symphytum Officinale with Metronidazole against P. gingivalis: An MIC and MBC Analysis." Open Dentistry Journal 18, no. 1 (2024). http://dx.doi.org/10.2174/0118742106299402240425053257.

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Background The RapID ANA II panel was used to evaluate bacterial responses, and the minimum inhibitory concentration (MIC) and minimum bactericidal concentration (MBC) were established. Aim This study aimed to investigate the antibacterial effects of Metronidazole, Symphytum Officinale, and Panax Ginseng on P. gingivalis Materials and Methods P. gingivalis strains, including strain ATCC 33277 and an isolate, were selected and prepared. A variety of test compounds, including Metronidazole, Symphytum Officinale, and Panax Ginseng, were procured and manufactured. A consistent technique was used t

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21

Ota, Tomoya, Wataru Saburi, Linda Elizabeth Jewell, Tom Hsiang, Ryozo Imai та Haruhide Mori. "Identification and characterization of extracellular GH3 β-glucosidase from the pink snow mold fungus, Microdochium nivale". Bioscience, Biotechnology, and Biochemistry, 13 квітня 2023. http://dx.doi.org/10.1093/bbb/zbad044.

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Abstract Glycoside hydrolase family 3 (GH3) β-glucosidase exists in many filamentous fungi. In phytopathogenic fungi, it is involved in fungal growth and pathogenicity. Microdochium nivale is a severe phytopathogenic fungus of grasses and cereals and is the causal agent of pink snow mold, but its β-glucosidase has not been identified. In this study, a GH3 β-glucosidase of M. nivale (MnBG3A) was identified and characterized. Among various p-nitrophenyl β-glycosides, MnBG3A showed activity on d-glucoside (pNP-Glc) and slight activity on d-xyloside. In the pNP-Glc hydrolysis, substrate inhibition

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22

Shim, Su-Hyeon, Bancha Mahong, Sang-Kyu Lee та ін. "Rice β-Glucosidase Os12BGlu38 is Required for Synthesis of Intine Cell Wall and Pollen Fertility". Journal of Experimental Botany, 27 вересня 2021. http://dx.doi.org/10.1093/jxb/erab439.

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Abstract Glycoside hydrolase family1 β-glucosidases play a variety of roles in plants, but their in planta functions are largely unknown in rice (Oryza sativa). In this study, the biological function of Os12BGlu38, a rice β-glucosidase, expressed in bicellular to mature pollen, was examined. Genotype analysis of progeny of self-fertilized heterozygous Os12BGlu38 T-DNA mutant, os12bglu38-1, found no homozygotes and a 1:1 ratio of wild type (WT) to heterozygotes. Reciprocal cross analysis demonstrated that Os12BGlu38 deficiency cannot be inherited through the male gamete. In cytological analysis

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23

Kamale, Chinmay, Abhishek Rauniyar та Prasenjit Bhaumik. "Rational design facilitates the improvement of glucose tolerance and catalytic properties of a β‐glucosidase from Acetivibrio thermocellus". FEBS Journal, 7 січня 2025. https://doi.org/10.1111/febs.17394.

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Cellulases are an ensemble of enzymes that hydrolyze cellulose chains into fermentable glucose and hence are widely used in bioethanol production. The last enzyme of the cellulose degradation pathway, β‐glucosidase, is inhibited by its product, glucose. The product inhibition by glucose hinders cellulose hydrolysis limiting the saccharification during bioethanol production. Thus, engineered β‐glucosidases with enhanced glucose tolerance and catalytic efficiency are essential. This study focuses on the rational engineering of β‐glucosidase from Acetivibrio thermocellus (WT‐AtGH1). Recombinant W

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24

Zhai, Xingyu, Kaijuan Wu, Rui Ji та ін. "Structure and Function Insight of the α-Glucosidase QsGH13 From Qipengyuania seohaensis sp. SW-135". Frontiers in Microbiology 13 (3 березня 2022). http://dx.doi.org/10.3389/fmicb.2022.849585.

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The α-glucosidases play indispensable roles in the metabolic mechanism of organism, prevention, and treatment of the disease, and sugar hydrolysis, and are widely used in chemical synthesis, clinical diagnosis, and other fields. However, improving their catalytic efficiency and production to meet commercial demand remains a huge challenge. Here we detected a novel GH13 family α-glucosidase, QsGH13, from the deep-sea bacterium Qipengyuania seohaensis sp. SW-135. QsGH13 is highly substrate specific and only hydrolyzes sugars containing alpha-1,4 glucoside bonds. For example, its enzymatic activi

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