ArticleBiotechnology for biofuels2016
Characterization of a glucose-tolerant β-glucosidase from Anoxybacillus sp. DT3-1.
Article in Biotechnology for biofuels, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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16 citing papers in PubMed, 55 citations in OpenAlex.
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- Release of Soybean Isoflavones by Using a β-Glucosidase from Alicyclobacillus herbarius.Chembiochem : a European journal of chemical biology · 2021Article
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- One-step purification of two novel thermotolerant β-1,4-glucosidases from a newly isolated strain of Fusarium chlamydosporum HML278 and their characterization.AMB Express · 2020Article
- A Novel High Glucose-Tolerant β-Glucosidase: Targeted Computational Approach for Metagenomic Screening.Frontiers in bioengineering and biotechnology · 2020Article
- Identification and molecular characterization of a psychrophilic GH1 β-glucosidase from the subtropical soil microorganism Exiguobacterium sp. GXG2.AMB Express · 2019Article
- Microbial Beta Glucosidase Enzymes: Recent Advances in Biomass Conversation for Biofuels Application.Biomolecules · 2019Review
- Microbial diversity of thermophiles with biomass deconstruction potential in a foliage-rich hot spring.MicrobiologyOpen · 2018Article
- Increased enzymatic hydrolysis of sugarcane bagasse by a novel glucose- and xylose-stimulated β-glucosidase from Anoxybacillus flavithermus subsp. yunnanensis E13BMC biochemistry · 2017Article
- Bioprospecting of novel thermostable β-glucosidase fromBiotechnology for biofuels · 2017Article
- When substrate inhibits and inhibitor activates: implications of β-glucosidases.Biotechnology for biofuels · 2017Article
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundIn general, biofuel production involves biomass pretreatment and enzymatic saccharification, followed by the subsequent sugar conversion to biofuel via fermentation. The crucial step in the production of biofuel from biomass is the enzymatic saccharification. Many of the commercial cellulase enzyme cocktails, such as Spezyme(®) CP (Genencor), Acellerase™ 1000 (Genencor), and Celluclast(®) 1.5L (Novozymes), are ineffectively to release free glucose from the pretreated biomass without additional β-glucosidase.
resultsIn this study, for the first time, a β-glucosidase DT-Bgl gene (1359 bp) was identified in the genome of Anoxybacillus sp. DT3-1, and cloned and heterologously expressed in Escherichia coli BL21. Phylogenetic analysis indicated that DT-Bgl belonged to glycosyl hydrolase (GH) family 1. The recombinant DT-Bgl was highly active on cello-oligosaccharides and p-nitrophenyl-β-d-glucopyranoside (pNPG). The DT-Bgl was purified using an Ni-NTA column, with molecular mass of 53 kDa using an SDS-PAGE analysis. It exhibited optimum activity at 70 °C and pH 8.5, and did not require any tested co-factors for activation. The K m and V max values for DT-Bgl were 0.22 mM and 923.7 U/mg, respectively, with pNPG as substrate. The DT-Bgl displayed high glucose tolerance, and retained 93 % activity in the presence of 10 M glucose.
conclusionsAnoxybacillus DT-Bgl is a novel thermostable β-glucosidase with low glucose inhibition, and converts long-chain cellodextrins to cellobiose, and further hydrolyse cellobiose to glucose. Results suggest that DT-Bgl could be useful in the development of a bioprocess for the efficient saccharification of lignocellulosic biomass.
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