ArticleApplied microbiology and biotechnology2020
Functional characterization of a novel thermophilic exo-arabinanase from Thermothielavioides terrestris.
Article in Applied microbiology and biotechnology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 24 citations in OpenAlex.
- The role of gut mycobiome in responses to cancer immunotherapy.Gut microbes · 2025Review
- Screening, Characterization and Comparison of Endoglucanases/Xylanases from Thermophilic Fungi: AInternational journal of molecular sciences · 2025Article
- Exo- and Endo-1,5-α-L-Arabinanases and Prebiotic Arabino-Oligosaccharides Production.Journal of microbiology and biotechnology · 2025Review
- Recombinant GH3 β-glucosidase stimulated by xylose and tolerant to furfural and 5-hydroxymethylfurfural obtained from Aspergillus nidulans.Bioresources and bioprocessing · 2024Article
- Secretome Analysis ofJournal of fungi (Basel, Switzerland) · 2024Article
- Advances in the production of fungi-derived lignocellulolytic enzymes using agricultural wastes.Mycology · 2024Review
- Review
- Arabinan hydrolysis by GH43 enzymes of Hungateiclostridium clariflavum and the potential synergistic mechanisms.Applied microbiology and biotechnology · 2022Article
- Arabinan saccharification by biogas reactor metagenome-derived arabinosyl hydrolases.Biotechnology for biofuels and bioproducts · 2022Article
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Authors and funding
14 authors at 6 institutions in 1 country.
Funding
Abstract
Arabinanases from glycoside hydrolase family GH93 are enzymes with exo-activity that hydrolyze the α-1,5 bonds between arabinose residues present on arabinan. Currently, several initiatives aiming to use byproducts rich in arabinan such as pectin and sugar beet pulp as raw material to produce various compounds of interest are being developed. However, it is necessary to use robust enzymes that have an optimal performance under pH and temperature conditions used in the industrial processes. In this work, the first GH93 from the thermophilic fungus Thermothielavioides terrestris (Abn93T) was heterologously expressed in Aspergillus nidulans, purified and biochemically characterized. The enzyme is a thermophilic glycoprotein (optimum activity at 70 °C) with prolonged stability in acid pHs (4.0 to 6.5). The presence of glycosylation affected slightly the hydrolytic capacity of the enzyme, which was further increased by 34% in the presence of 1 mM CoCl
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