ArticleAMB Express2016
Cloning a novel endo-1,4-β-D-glucanase gene from Trichoderma virens and heterologous expression in E. coli.
Article in AMB Express, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 14 citations in OpenAlex.
- Advances, challenges, and future directions towards a cellulolytic Escherichia coli.Biotechnology for biofuels and bioproducts · 2026Review
- Fungal cellulases: a comprehensive review on production, innovations, and applications.Archives of microbiology · 2026Review
- Heterologous expression, molecular studies and biochemical characterization of a novel alkaline esterase gene fromRSC advances · 2022Article
- Heterologous expression and characterization of glycoside hydrolase with its potential applications in hyperthermic environment.Saudi journal of biological sciences · 2022Article
- Soluble expression of recombinant active cellulase in E.coli using B.subtilis (natto strain) cellulase gene.Journal, genetic engineering & biotechnology · 2021Article
- Optimized soluble expression of a novel endoglucanase from3 Biotech · 2020Article
- Identification and characterization of an Endo-glucanase secreted from cellulolytic Escherichia coli ZH-4.BMC biotechnology · 2019Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Endo-1,4-β-D-glucanase (EG), as a key constituent of cellulase taking the responsibility of cutting β-1,4 glycosidic bonds, plays the essential role in the process of degrading cellulose by cellulase. Cloning and expressing the EG gene is important to the cellulase research and application. In this work, a novel EG gene was cloned from Trichoderma virens ZY-01, which was a cellulase secreting microbe isolated by our laboratory. The DNA sequence showed that the length of the cloned EG is 1069 bp, which had 95.2% similarity to the EG IV from T. viride AS 3.3711. Further, the expression vector pET-32a-EG was constructed and was successfully heterologously expressed in Escherichia coli. The expression product was purified with Ni
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