ArticleBrazilian journal of microbiology : [publication of the Brazilian Society for Microbiology]
Cloning and expression of an endoglucanase gene from the thermotolerant fungus Aspergillus fumigatus DBiNU-1 in Kluyveromyces lactis.
Article in Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology]. 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, 23 citations in OpenAlex.
- Antifungal activity of Burkholderia sensu lato metabolites against coffee phytopathogens: evidence of chemical diversity.World journal of microbiology & biotechnology · 2026Article
- Powerful cell wall biomass degradation enzymatic system from saprotrophicCell surface (Amsterdam, Netherlands) · 2024Review
- Advances in the production of fungi-derived lignocellulolytic enzymes using agricultural wastes.Mycology · 2024Review
- Review
- Thermostable Cellulases / Xylanases From Thermophilic and Hyperthermophilic Microorganisms: Current Perspective.Frontiers in bioengineering and biotechnology · 2021Review
- Surveying of acid-tolerant thermophilic lignocellulolytic fungi in Vietnam reveals surprisingly high genetic diversity.Scientific reports · 2019Article
- Functional Expression of a Thermostable Endoglucanase from Thermoascus aurantiacus RCKK in Pichia pastoris X-33 and Its Characterization.Molecular biotechnology · 2018Article
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Authors and funding
5 authors at 3 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
An intronless endoglucanase from thermotolerant Aspergillus fumigatus DBINU-1 was cloned, characterized and expressed in the yeast Kluyveromyces lactis. The full-length open reading frame of the endoglucanase gene from A. fumigatus DBiNU-1, designated Cel7, was 1383 nucleotides in length and encoded a protein of 460 amino acid residues. The predicted molecular weight and the isoelectric point of the A. fumigatus Cel7 gene product were 48.19kDa and 5.03, respectively. A catalytic domain in the N-terminal region and a fungal type cellulose-binding domain/module in the C-terminal region were detected in the predicted polypeptide sequences. Furthermore, a signal peptide with 20 amino acid residues at the N-terminus was also detected in the deduced amino acid sequences of the endoglucanase from A. fumigatus DBiNU-1. The endoglucanase from A. fumigatus DBiNU-1 was successfully expressed in K. lactis, and the purified recombinant enzyme exhibited its maximum activity at pH 5.0 and 60°C. The enzyme was very stable in a pH range from 4.0 to 8.0 and a temperature range from 30 to 60°C. These features make it suitable for application in the paper, biofuel, and other chemical production industries that use cellulosic materials.
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