Production of ß-Glucosidase by Penicillium purpurogenum

Dhake, A.B.; Patil, M. B.

doi:10.1590/s1517-83822005000200013

Cited by 31 publications

(18 citation statements)

References 18 publications

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“…• C. This is in agreement with the findings of Riou et al (1998) and Dhake & Patil (2005), while Choi et al (2009) ther increase in temperature resulted in the decrease in activity and coagulation of enzyme occurring at 60 However, Wright et al (1992) and Christakopoulos et al (1995) obtainted maximum β-glucosidase activity at 60…”

supporting

confidence: 90%

“…Choi et al (2009) obtained maximum B. licheniformis β-glucosidase activity at pH 6 with citrate phosphate buffer. The activities of β-glucosidases from Penicillium purpurogenum, Clostridium strain RT 9 and Cellulomonas biazotea NIAB 442 were maximal at pH 4.5, 5.5 and 6.6, respectively (Tabassum et al 1992;Siddiqui et al 1997a;Dhake & Patil 2005).…”

Section: Characterization Of Recombinant β-Glucosidasementioning

confidence: 98%

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Cloning and expression of β-glucosidase gene from Bacillus licheniformis into E. coli BL 21 (DE3)

et al. 2011

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A 1.4 Kb fragment of Bacillus licheniformis ATCC 14580 encoding β-glucosidase was cloned and expressed in Escherichia coli. β-Glucosidase expressed by E. coli harboring cloned gene was located entirely in the intracellular fraction. Recombinant β-glucosidase protein was purified to homogeneity level and the molecular weight was found to be 53 kDa using sodium dodecyl sulfate polyacrylamide gel electrophoresis analysis. It gave maximum activity at 50• C and pH 6. Km and Vmax were 0.206 mM and 1.26 U/mg, respectively, with p-nitrophenyl-β-D-glucopyranoside, while activation energy Ea, enthalpy of activation ∆H and entropy of activation ∆S were found to be 66.31 kJ/mol, 64.04 kJ/mol and 48.28 J/mol/K, respectively. The pKa1 and pKa2 of the ionizable groups of active site residues involved in Vmax were found to be 5.5 and 7.0, respectively. When the recombinant β-glucosidase protein was used as a member of consortium with endoglucanase and exoglucanase for the saccharification of wheat straw, 123% increase in saccharification was observed.

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supporting

confidence: 90%

Section: Characterization Of Recombinant β-Glucosidasementioning

confidence: 98%

Cloning and expression of β-glucosidase gene from Bacillus licheniformis into E. coli BL 21 (DE3)

et al. 2011

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“…Pericin and Jarak (1995) obtained maximum β-glucosidase activity from Diaporthe (Phomopsis) helianthi at pH 4.8. In contrast, Leite et al (2007) obtained maximum activity of β-glucosidase from Thermoascus aurantiacus at pH 4.5 while Hang and Woodams (1994), Karnchanatat et al (2007), Dhake and Patil (2005) and Zanoelo et al (2004) obtained maximum β-glucosidase activity from Aspergillus Foetidus, Daldinia eschscholzii, Penicillium purpurogenum and Scytalidum thermophilum at pH 4.6, 5.0, 5.5 and 6.5 respectively. The change in pH affects the ionization of essential active site amino acid residues, which are involved in substrate binding and catalysis, that is, breakdown of substrate into products.…”

Section: Enzyme Characterizationmentioning

confidence: 86%

Metabolic engineering and thermodynamic characterization of an extracellular -glucosidase produced by Aspergillus niger

Zahoor¹,

Javed²,

Aftab³

et al. 2011

Afr. J. Biotechnol.

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The production of an extracellular β-glucosidase by Aspergillus niger NRRL 599 was optimized using submerged fermentation technique. Effect of different media, different carbon sources, initial pH of the fermentation medium, temperature, incubation period and inoculum size on the production of β-glucosidase enzyme was investigated. A. niger NRRL 599 produced maximum extracellular β-glucosidase (4.48 U/mg) in Eggins and Pugh medium with 1% wheat bran (w/v) at pH 5.5 inoculated with 4% conidial suspension after 96 h of incubation at 30°C. Purified β-glucosidase gave K m and V max values of 3.11 mM and 20.83 U/mg respectively for pNPG hydrolysis. The enzyme was optimally active at pH 4.8 and at temperature of 60°C. Thermodynamic parameters, E a , ∆H and ∆S were found to be 52.17 KJ/mol, 49.90 J/mol.K and -71.69 KJ/mol, respectively. The pKa 1 and pKa 2 of ionizable groups of active site residues involved in V max were calculated to be 4.1 and 6.0 respectively.

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“…For example, β-glucosidases exhibiting optimal activity at temperature of 50°C have been identified from Flammulina velutipes [113], Daldinia eschscholzii [65], Penicillium purpurogenum [114] and those with optimal activity at 60°C have been reported from Ceriporiopsis subvermispora [115], and Halothermothrix orenii [116]. β-Glucosidase with optimal activity at 70°C has been reported from A. niger KCCM 11239 [117], and T. aurantiacus IFO9748 [43].…”

Section: Ph and Temperature Optimamentioning

confidence: 99%

Microbial β-Glucosidases: Screening, Characterization, Cloning and Applications

Ahmed¹,

Aslam²,

Ashraf³

et al. 2017

JAEM

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Cellulose is the most abundant biomaterial in the biosphere and the major component of plant biomass.Cellulase is an enzymatic system required for conversion of renewable cellulose biomass into free sugar for subsequent use in different applications. Cellulase system mainly consists of three individual enzymes namely: endoglucanase, exoglucanase and β-glucosidases. β-Glucosidases are ubiquitous enzymes found in all living organisms with great biological significance. β-Glucosidases have also tremendous biotechnological applications such as biofuel production, beverage industry, food industry, cassava detoxification and oligosaccharides synthesis. Microbial β-glucosidases are preferred for industrial uses because of robust activity and novel properties exhibited by them. This review aims at describing the various biochemical methods used for screening and evaluating β-glucosidases activity from microbial sources. Subsequently, it generally highlights techniques used for purification of β-glucosidases. It then elaborates various biochemical and molecular properties of this valuable enzyme such as pH and temperature optima, glucose tolerance, substrate specificity, molecular weight, and multiplicity. Furthermore, it describes molecular cloning and expression of bacterial, fungal and metagenomic β-glucosidases. Finally, it highlights the potential biotechnological applications of β-glucosidases.

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Production of ß-Glucosidase by Penicillium purpurogenum

Cited by 31 publications

References 18 publications

Cloning and expression of β-glucosidase gene from Bacillus licheniformis into E. coli BL 21 (DE3)

Cloning and expression of β-glucosidase gene from Bacillus licheniformis into E. coli BL 21 (DE3)

Metabolic engineering and thermodynamic characterization of an extracellular -glucosidase produced by Aspergillus niger

Microbial β-Glucosidases: Screening, Characterization, Cloning and Applications

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