ArticlePloS one2019
Characterization of two thermophilic cellulases from Talaromyces leycettanus JCM12802 and their synergistic action on cellulose hydrolysis.
Article in PloS one, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 36 citations in OpenAlex.
- Fungal cellulases: a comprehensive review on production, innovations, and applications.Archives of microbiology · 2026Review
- Heterologous Expression of Thermostable Endoglucanases from Rasamsonia emersonii: A Paradigm Shift in Biomass Hydrolysis.Applied biochemistry and biotechnology · 2025Article
- An Investigation of the Secretome Composition ofInternational journal of molecular sciences · 2025Article
- Expression and characterization of a novel microbial GH9 glucanase, IDSGLUC9-4, isolated from sheep rumen.Animal bioscience · 2024Article
- Enhanced crystalline cellulose degradation by a novel metagenome-derived cellulase enzyme.Scientific reports · 2024Article
- Microbial β-glucanases: production, properties, and engineering.World journal of microbiology & biotechnology · 2023Review
- Enhancement of catalytic activity and alkaline stability of cellobiohydrolase by structure-based protein engineering.3 Biotech · 2022Article
- Recombinant cellobiohydrolase of Myceliophthora thermophila: characterization and applicability in cellulose saccharification.AMB Express · 2021Article
- Improvement of thermostability and catalytic efficiency of glucoamylase from Talaromyces leycettanus JCM12802 via site-directed mutagenesis to enhance industrial saccharification applications.Biotechnology for biofuels · 2021Article
- A Novel Dimeric Exoglucanase (GH5_38): Biochemical and Structural Characterisation towards its Application in Alkyl Cellobioside Synthesis.Molecules (Basel, Switzerland) · 2020Article
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8 authors at 2 institutions in 1 country.
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Abstract
Talaromyces leycettanus JCM12802 is a great producer of thermophilic glycoside hydrolases (GHs). In this study, two cellulases (TlCel5A and TlCel6A) belonging to GH5 and GH6 respectively were expressed in Pichia pastoris and functionally characterized. The enzymes had acidic and thermophilic properties, showing optimal activities at pH 3.5-4.5 and 75-80°C, and retained stable at temperatures up to 60°C and over a broad pH range of 2.0-8.0. TlCel5A and TlCel6A acted against several cellulose substrates with varied activities (3,101.1 vs. 92.9 U/mg to barley β-glucan, 3,905.6 U/mg vs. 109.0 U/mg to lichenan, and 840.3 and 0.09 U/mg to CMC-Na). When using Avicel, phosphoric acid swollen cellulose (PASC) or steam-exploded corn straw (SECS) as the substrate, combination of TlCel5A and TlCel6A showed significant synergistic action, releasing more reduced sugars (1.08-2.87 mM) than the individual enzymes. These two cellulases may represent potential enzyme additives for the efficient biomass conversion and bioethanol production.
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