ArticleScientific reports2017
Identification and characterization of a novel β-glucosidase via metagenomic analysis of Bursaphelenchus xylophilus and its microbial flora.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 38 citations in OpenAlex.
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- A novel GH3-β-glucosidase from soda lake metagenomic libraries with desirable properties for biomass degradation.Scientific reports · 2024Article
- Exploring the microbial diversity and characterization of cellulase and hemicellulase genes in goat rumen: a metagenomic approach.BMC biotechnology · 2023Article
- A glucose tolerant β-glucosidase from a newly isolated Neofusicoccum parvum strain F7: production, purification, and characterization.Scientific reports · 2023Article
- Screening for cellulases and preliminary optimisation of glucose tolerant β-glucosidase production and characterisation.Mycology · 2023Article
- A Paper-Based Analytical Device Integrated with Smartphone: Fluorescent and Colorimetric Dual-Mode Detection of β-Glucosidase Activity.Biosensors · 2022Article
- Discovery of novel carbohydrate degrading enzymes from soda lakes through functional metagenomics.Frontiers in microbiology · 2022Article
- Scions impact biomass allocation and root enzymatic activity of rootstocks in grafted melon and watermelon plants.Frontiers in plant science · 2022Article
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- The Goldilocks Approach: A Review of Employing Design of Experiments in Prokaryotic Recombinant Protein Production.Bioengineering (Basel, Switzerland) · 2018Review
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
β-glucosidases catalyze the final step of cellulose hydrolysis and are essential in cellulose degradation. A β-glucosidase gene, cen502, was identified and isolated from a metagenomic library from Bursaphelenchus xylophilus via functional screening. Analyses indicated that cen502 encodes a 465 amino acid polypeptide that contains a catalytic domain belonging to the glycoside hydrolase family 1 (GH1). Cen502 was heterologously expressed, purified, and biochemically characterized. Recombinant Cen502 displayed optimum enzymatic activity at pH 8.0 and 38 °C. The enzyme had highest specific activity to p-nitrophenyl-β-D-glucopyranoside (pNPG; 180.3 U/mg) and had K
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