ArticleApplied and environmental microbiology2013
Processivity and enzymatic mode of a glycoside hydrolase family 5 endoglucanase from Volvariella volvacea.
Article in Applied and environmental microbiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 91 citations in OpenAlex.
- A Thermostable Multifunctional GH5 Endoglucanase From Bacillus sp. for Lignocellulosic Biomass Saccharification.Biotechnology journal · 2026Article
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- HisAMB Express · 2025Article
- A novel AA14 LPMO from Talaromyces rugulosus with bifunctional cellulolytic/hemicellulolytic activity boosted cellulose hydrolysis.Biotechnology for biofuels and bioproducts · 2024Article
- Molecular dynamics-based structural insights of the first putative endoglucanase, PsGH5A of glycoside hydrolase family 5 from Pseudopedobacter saltans.Journal of molecular modeling · 2023Article
- Experimental evidence for enzymatic cell wall dissolution in a microbial protoplast feeder (Orciraptor agilis, Viridiraptoridae).BMC biology · 2022Article
- Comparison of the Biochemical Properties and Roles in the Xyloglucan-Rich Biomass Degradation of a GH74 Xyloglucanase and Its CBM-Deleted Variant fromInternational journal of molecular sciences · 2022Article
- Fungal cellulases: protein engineering and post-translational modifications.Applied microbiology and biotechnology · 2022Review
- Two C1-oxidizing AA9 lytic polysaccharide monooxygenases from Sordaria brevicollis differ in thermostability, activity, and synergy with cellulase.Applied microbiology and biotechnology · 2021Article
- Application of surfactants in papermaking industry and future development trend of green surfactants.Applied microbiology and biotechnology · 2021Review
- Bioconversion of bamboo shoot shells through the cultivation of the edible mushrooms Volvariella volvacea.Ecotoxicology (London, England) · 2021Article
- Structures of two novel crystal forms of Aspergillus oryzae alpha amylase (taka-amylase).Journal of bioscience and bioengineering · 2021Article
- Enhanced Enzymatic Hydrolysis of Cellulose From Substrate and Indole-3-Acetic Acid Content-During the Fruiting Body Differentiation Stage by Sodium Acetate Addition.Frontiers in fungal biology · 2021Article
- Carbohydrate Binding Modules: Diversity of Domain Architecture in Amylases and Cellulases From Filamentous Microorganisms.Frontiers in bioengineering and biotechnology · 2020Review
- A processive endoglucanase with multi-substrate specificity is characterized from porcine gut microbiota.Scientific reports · 2019Article
- A Novel Subfamily of Endo-β-1,4-Glucanases in Glycoside Hydrolase Family 10.Applied and environmental microbiology · 2019Article
- An F-type lectin domain directs the activity of Streptosporangium roseum alpha-l-fucosidase.Glycobiology · 2018Article
- Article
- Altering the linker in processive GH5 endoglucanase 1 modulates lignin binding and catalytic properties.Biotechnology for biofuels · 2018Article
- Processivity and enzymatic mechanism of a multifunctional family 5 endoglucanase fromBiotechnology for biofuels · 2018Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
EG1 is a modular glycoside hydrolase family 5 endoglucanase from Volvariella volvacea consisting of an N-terminal carbohydrate-binding module (CBM1) and a catalytic domain (CD). The ratios of soluble to insoluble reducing sugar produced from filter paper after 8 and 24 h of exposure to EG1 were 6.66 and 8.56, respectively, suggesting that it is a processive endoglucanase. Three derivatives of EG1 containing a core domain only or additional CBMs were constructed in order to evaluate the contribution of the CBM to the processivity and enzymatic mode of EG1 under stationary and agitated conditions. All four enzymatic forms exhibited the same mode of action on both soluble and insoluble cellulosic substrates with cellobiose as a main end product. An additional CBM fused at either the N or C terminus reduced specific activity toward soluble and insoluble celluloses under stationary reaction conditions. Deletion of the CBM significantly decreased enzyme processivity. Insertion of an additional CBM also resulted in a dramatic decrease in processivity in enzyme-substrate reaction mixtures incubated for 0.5 h, but this effect was reversed when reactions were allowed to proceed for longer periods (24 h). Further significant differences were observed in the substrate adsorption/desorption patterns of EG1 and enzyme derivatives equipped with an additional CBM under agitated reaction conditions. An additional family 1 CBM improved EG1 processivity on insoluble cellulose under highly agitated conditions. Our data indicate a strong link between high adsorption levels and low desorption levels in the processivity of EG1 and possibly other processive endoglucanses.
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