Characterization of a recombinant aryl β-glucosidase from Neosartorya fischeri NRRL181

Kalyani, Dayanand; Lee, Kyoung-Mi; Tiwari, Manish Kumar; Priyadharshini, R.; Kim, Hoon; Kim, In-Won; Jeya, Marimuthu; Lee, Jung-Kul

doi:10.1007/s00253-011-3631-6

Cited by 18 publications

(8 citation statements)

References 44 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%

“…Cellobiase has been identified from Cellulomonas biazotea [124], and A. niger [52]. Aryl-β-D-glucosidase has been reported in N. fischeri NRRL181 [86] and A. oryzae [125]. Further studies, including molecular docking studies, are needed to determine interactions between amino acids residues with substrates which may provide an insight into these substrate specificities and allow better use of this multifunctional biocatalyst [126,127].…”

Section: Substrate Specificitymentioning

confidence: 99%

“…For instance, β-glucosidase from Anoxybacillus sp. DT3-1 [83], Exiguobacterium antarcticum B7 [84], and Thermoanaerobacterium thermosaccharolyticum DSM 571 [85] has been expressed in E. coli as fusion protein with six His tag at N-terminal and purified through Nickel-Nitrilotriacetic acid (Ni-NTA) chromatography [85,86,87]. Glutathione-S-Transferase (GST) affinity has been used for purification of recombinant β-glucosidase from Exiguobacterium oxidotolerans A011 expressed as fusion protein with GST which provides additional advantage by acting as a chaperone protein to facilitate protein folding, and provide a mean for their purification by immobilized glutathione column [88,89].…”

Section: Purification Of β-Glucosidasementioning

confidence: 99%

“…Generally fungal β-glucosidase exhibits optimal activity at pH of 4.0-6.0 [59, 69,86,92,93], nevertheless β-glucosidase with optimal pH of 2.4 has been reported from T. cylindrosporum Syzx4 [68] and that with optimal pH of 9 and 10 has been reported from Acremonium murorun LPSC 927 and Chaetomium globosum, respectively [94,95]. Bacterial β-glucosidase exhibits optimal activity at pH of 6-7 [44,87,96,97], although those with pH optima of 5, 8 and 10 has been reported from Caldicellulosiruptor saccharolyticus [98], Bacillus halodurans [99], Klebsiella pneumoniae [100], respectively.…”

Section: Ph and Temperature Optimamentioning

confidence: 99%

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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%

Section: Substrate Specificitymentioning

confidence: 99%

Section: Purification Of β-Glucosidasementioning

confidence: 99%

Section: Ph and Temperature Optimamentioning

confidence: 99%

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

Ahmed¹,

Aslam²,

Ashraf³

et al. 2017

JAEM

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“…The optimum temperature of BGL-A3 (50 BGL-A1, BGL-A2, and BGL-A3 showed absolute substrate specificity for pNPG but negligible activities for other substrates, including cellobiose. This finding suggests BGL-A1, BGL-A2, and BGL-A3 are typical aryl β-glucosidases, like those from A. sydowii BTMFS 55 [32], Neosartorya fischeri NRRL181 [33], Phialophora sp. G5 [34], and Aspergillus sp.…”

Section: Discussionmentioning

confidence: 87%

Characterization of Three Extracellular ��-Glucosidases Produced by a Fungal Isolate Aspergillus sp. YDJ14 and Their Hydrolyzing Activity for a Flavone Glycoside

Oh¹,

Lee²,

Baek³

et al. 2018

Journal of Microbiology and Biotechnology

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A cellulolytic fungus, YDJ14, was isolated from compost and identified as an sp. strain. Three extracellular β-glucosidases, BGL-A1, BGL-A2, and BGL-A3, were separated using ultrafiltration, ammonium sulfate fractionation, and High-Q chromatography. The molecular masses of the three enzymes were estimated to be 100, 45, and 40 kDa, respectively, by SDS-PAGE. The optimum pH and temperature of BGL-A3 were 5.0 and 50°C, respectively, whereas the optimum pH and temperature of BGL-A1 and BGL-A2 were identical (4.0 and 60°C, respectively). The half-life of BGL-A3 at 70°C (2.8 min) was shorter than that of BGL-A1 and BGL-A2 (12.1 and 8.8 min, respectively). All three enzymes preferred-nitrophenyl-β--glucopyranoside (NPG) and hardly hydrolyzed cellobiose, suggesting that these enzymes were aryl β-glucosidases. The of BGL-A3 (1.26 mM) forNPG was much higher than that of BGL-A1 and BGL-A2 (0.25 and 0.27 mM, respectively). These results suggested that BGL-A1 and BGL-A2 were similar in their enzymatic properties, whereas BGL-A3 differed from the two enzymes. When tilianin (a flavone glycoside of acacetin) was reacted with the three enzymes, the inhibitory activity for monoamine oxidase, a target in the treatment of neurological disorders, was similar to that shown by acacetin. We conclude that these enzymes may be useful in the hydrolysis of flavone glycosides to improve their inhibitory activities.

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