ArticlePloS one2013
Engineering of family-5 glycoside hydrolase (Cel5A) from an uncultured bacterium for efficient hydrolysis of cellulosic substrates.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Enhanced crystalline cellulose degradation by a novel metagenome-derived cellulase enzyme.Scientific reports · 2024Article
- Multidomain chimeric enzymes as a promising alternative for biocatalysts improvement: a minireview.Molecular biology reports · 2024Review
- Characterization of two GH5 endoglucanases from termite microbiome using synthetic metagenomics.Applied microbiology and biotechnology · 2020Article
- Engineering Robust Cellulases for Tailored Lignocellulosic Degradation Cocktails.International journal of molecular sciences · 2020Review
- Cellulolytic thermophilic microorganisms in white biotechnology: a review.Folia microbiologica · 2020Review
- Controlled Aggregation and Increased Stability of β-Glucuronidase by Cellulose Binding Domain Fusion.PloS one · 2017Article
- The Quaternary Structure of a Glycoside Hydrolase Dictates Specificity toward β-Glucans.The Journal of biological chemistry · 2016Article
- Cloning, Expression, and Characterization of a Thermophilic Endoglucanase, AcCel12B from Acidothermus cellulolyticus 11B.International journal of molecular sciences · 2015Article
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Authors and funding
11 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cel5A, an endoglucanase, was derived from the metagenomic library of vermicompost. The deduced amino acid sequence of Cel5A shows high sequence homology with family-5 glycoside hydrolases, which contain a single catalytic domain but no distinct cellulose-binding domain. Random mutagenesis and cellulose-binding module (CBM) fusion approaches were successfully applied to obtain properties required for cellulose hydrolysis. After two rounds of error-prone PCR and screening of 3,000 mutants, amino acid substitutions were identified at various positions in thermotolerant mutants. The most heat-tolerant mutant, Cel5A_2R2, showed a 7-fold increase in thermostability. To enhance the affinity and hydrolytic activity of Cel5A on cellulose substrates, the family-6 CBM from Saccharophagus degradans was fused to the C-terminus of the Cel5A_2R2 mutant using overlap PCR. The Cel5A_2R2-CBM6 fusion protein showed 7-fold higher activity than the native Cel5A on Avicel and filter paper. Cellobiose was a major product obtained from the hydrolysis of cellulosic substrates by the fusion enzyme, which was identified by using thin layer chromatography analysis.
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