Characterization of β-glucosidase from a strain of Penicillium purpurogenum KJS506

Jeya, Marimuthu; Joo, Ah-Reum; Lee, Kyoung-Mi; Tiwari, Manish Kumar; Lee, Kyoung-Min; Kim, Sang‐Hwan; Lee, Jung-Kul

doi:10.1007/s00253-009-2395-8

Cited by 78 publications

(43 citation statements)

References 36 publications

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“…Moreover, hyperthermophilic β-glucosidase has been identified from Pyrococcus furiosus with optimal temperature of 102-105°C [63] and β-glucosidase with optimal activity at 90°C has also been identified from hot spring metagenome and termite gut metagenome [105,107]. Mesophilic β-glucosidase has been reported from Neocallimastix patriciarum W5 [118], Neosartorya fischeri NRRL181 [86], and P. purpurogenum KJS506 [119] with optimal temperature of 40, and 32°C, respectively. Cold active β-glucosidase have been characterized from Paenibacillus sp.…”

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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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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“…respectively. However, Christakopoulos et al (1995) and Jeya et al (2010) obtained maximum β-glucosidase activity at 65°C from Fusarium oxysporum and Penicillium Purpurogenum respectively. Thermodynamic studies of β-glucosidase were carried out using Arrhenius plot and activation energy (E a ), change in enthalpy (∆H) and change in entropy (∆S) were calculated to be 52.17 KJ/mol, 49.90 KJ/mol and -71.69 J/mol.K respectively (Figures 8 and 9).…”

Section: Enzyme Characterizationmentioning

confidence: 99%

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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“…Cellulose hydrolysis is affected by the synergistic action of various cellulases, including endoglucanase (EG), cellobiohydrolase (CBH), and β-glucosidase (BGL). Although BGL does not actually hydrolyze cellulose, the enzyme plays an important role in cellulose hydrolysis: BGL efficiently eliminates end-product inhibition by cellobiose (Jeya et al 2010), increasing the rate of cellulose hydrolysis. Singh and Bishnoi (2012) reported an increase in sugar yield with increased BGL loading.…”

Section: Introductionmentioning

confidence: 99%

Optimization of Medium Components for β-glucosidase Production in Schizophyllum commune KUC9397 and Enzymatic Hydrolysis of Lignocellulosic Biomass

Lee¹,

Lee²,

Kim³

et al. 2014

BioResources

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Medium components for β-glucosidase (BGL) production in Schizophyllum commune KUC9397 were optimized using a central composite design and response surface methodology. From the various medium components tested, cellulose, soy peptone, and thiamine HCl were selected as the optimal carbon, nitrogen, and vitamin sources, respectively. The highest BGL production was obtained with 2.96% cellulose, 2.30% soy peptone, and 0.11% thiamine HCl. BGL production in the optimized medium was increased 7.2-fold compared to production in an unoptimized medium. Crude enzyme preparation from S. commune KUC9397 was used to saccharify pretreated lignocellulosic biomass. The crude enzyme preparations showed statistically equal saccharification rates as Cellobiase, a commercial BGL. This finding indicates that crude enzymes produced by S. commune KUC9397 have good potential for application in cellulosic biomass conversion systems in place of Cellobiase.

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Characterization of β-glucosidase from a strain of Penicillium purpurogenum KJS506

Cited by 78 publications

References 36 publications

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

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

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

Optimization of Medium Components for β-glucosidase Production in Schizophyllum commune KUC9397 and Enzymatic Hydrolysis of Lignocellulosic Biomass

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