Purification and characterization of ß-glucosidase from Melanocarpus sp. MTCC 3922

Kaur, Jatinder; Chadha, Bhupinder Singh; Kumar, Badhan A.; Ghatora, Sonia; Saini, Harvinder Singh

doi:10.2225/vol10-issue2-fulltext-4

Cited by 85 publications

(61 citation statements)

References 22 publications

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“…Further increase in temperature resulted in decreased β-glucosidase activity. Kimura et al (1999) and Kaur et al (2007) also obtained maximum β-glucosidase activity at 60°C from Aspergillus sojae and Melanocarpus sp. respectively.…”

Section: Enzyme Characterizationmentioning

confidence: 86%

“…mg respectively were calculated for pNPG hydrolysis by β-glucosidase from the Melanocarpus sp. by Kaur et al (2007). The K m and V max values for pNPG hydrolysis for Humicola insolens β-glucosidase were calculated to be 0.16 mM and 18.1 U/mg respectively (Souza et al, 2010).…”

Section: Enzyme Characterizationmentioning

confidence: 99%

“…β-Glucosidase is generally responsible for the regulation of the whole cellulolytic process and is a rate-limiting factor during enzymatic hydrolysis of cellulose, as both endoglucanase and exoglucanase activities are often inhibited by cellobiose. Thus, β-glucosidase not only produces glucose from cellobiose, but also reduces cellobiose inhibition, allowing endoglucanase and exoglucanase enzymes to function more efficiently (Kaur et al, 2007). Supplementing β-glucosidase in commercial cellulase preparations has been reported to result in increased rate of cellulose hydrolysis and ethanol production (Wallecha and Mishra, 2003).…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

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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Section: Enzyme Characterizationmentioning

confidence: 86%

Section: Enzyme Characterizationmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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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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“…MTCC 3922 [148], T. clypeatus [149], and compost microbial metagenome [108]. Understanding mechanism of transglycosylation and identification of amino acid residues playing central role in transglycosylation reactions hold a great importance in protein engineering for the development of β-glucosidase with high transglycosylation reaction.…”

Section: Transglycosylation Activitymentioning

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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“…Although, a large diversity of microorganisms can produce cellulase enzymes (Duff and Murray, 1996;Kaur et al 2007;Villena and Gutiérrez-Correa, 2007), the cellulase system of the filamentous fungus Trichoderma reesei has been found to be one of the most effective for hydrolysis of cellulosic materials. T. reesei produces an extracellular, stable, and efficient cellulase enzyme system (Tengborg et al 2001;Lynd et al 2002).…”

Section: *Corresponding Authormentioning

confidence: 99%

Influence of buffer systems on Trichoderma reesei Rut C-30 morphology and cellulase production

Ferreira¹,

Duarte²,

Queiroz³

et al. 2009

Electro Journal of Biotech

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The cellulase enzyme production is a key issue in the enzymatic hydrolysis of lignocellulosic materials. Since fungal morphology influences the productivity of fungal fermentations, it is of major importance to well know the fungal behavior during culture for cellulase production. In this work, the influence of medium supplementation, with different buffer systems at two different concentrations and pH conditions, on the morphology of T. reesei Rut C-30 and cellulase production, was investigated. A medium without buffer was used as control. The results suggest that fungal morphology is significantly dependent on the addition of different buffer systems to the nutrient broth. The mycelial morphology shows a clear transition from clumped to pelleted forms in cultures with variation of buffer systems and concentration. The higher filter paper activity was obtained using 100 mM succinate buffer, at pH 4.8, in the medium supplementation, corresponding to a dispersed mycelial morphology.

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Purification and characterization of ß-glucosidase from Melanocarpus sp. MTCC 3922

Cited by 85 publications

References 22 publications

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

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

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

Influence of buffer systems on Trichoderma reesei Rut C-30 morphology and cellulase production

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