ArticleMolecules (Basel, Switzerland)2020
A Novel Dimeric Exoglucanase (GH5_38): Biochemical and Structural Characterisation towards its Application in Alkyl Cellobioside Synthesis.
Article in Molecules (Basel, Switzerland), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 9 citations in OpenAlex.
- Utilisation of mango seed husk for the production of phenolic compounds and glucose with C1184 enzyme preparation reveals the role of glucuronoyl esters in lignin-carbohydrate linkages in biomass recalcitrance.Bioresources and bioprocessing · 2025Article
- Lichenase and Cellobiohydrolase Activities of a Novel Bi-Functional β-Glucanase from the Marine BacteriumMarine drugs · 2024Article
- Microbial β-glucanases: production, properties, and engineering.World journal of microbiology & biotechnology · 2023Review
- Recent advances in enzymatic synthesis of β-glucan and cellulose.Carbohydrate research · 2021Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
An exoglucanase (Exg-D) from the glycoside hydrolase family 5 subfamily 38 (GH5_38) was heterologously expressed and structurally and biochemically characterised at a molecular level for its application in alkyl glycoside synthesis. The purified Exg-D existed in both dimeric and monomeric forms in solution, which showed highest activity on mixed-linked β-glucan (88.0 and 86.7 U/mg protein, respectively) and lichenin (24.5 and 23.7 U/mg protein, respectively). They displayed a broad optimum pH range from 5.5 to 7 and a temperature optimum from 40 to 60 °C. Kinetic studies demonstrated that Exg-D had a higher affinity towards β-glucan, with a
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.