ArticleApplied and environmental microbiology2000
Imaging the enzymatic digestion of bacterial cellulose ribbons reveals the endo character of the cellobiohydrolase Cel6A from Humicola insolens and its mode of synergy with cellobiohydrolase Cel7A.
Article in Applied and environmental microbiology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.
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55 citing papers in PubMed.
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- Thermotolerance Mechanism of Fungal GH6 Cellobiohydrolase. Part I. Characterization of Thermotolerant Mutant from the BasidiomyceteJournal of applied glycoscience · 2024Article
- Thermotolerance Mechanism of Fungal GH6 Cellobiohydrolase. Part II. Structural Analysis of Thermotolerant Mutant from the BasidiomyceteJournal of applied glycoscience · 2024Article
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- Processive Enzymes Kept on a Leash: How Cellulase Activity in Multienzyme Complexes Directs Nanoscale Deconstruction of Cellulose.ACS catalysis · 2021Article
- Oxidized Product Profiles of AA9 Lytic Polysaccharide Monooxygenases Depend on the Type of Cellulose.ACS sustainable chemistry & engineering · 2021Article
- Review
- Biocontrol of Two Bacterial Inoculant Strains and Their Effects on the Rhizosphere Microbial Community of Field-Grown Wheat.BioMed research international · 2021Article
- The Nanofication and Functionalization of Bacterial Cellulose and Its Applications.Nanomaterials (Basel, Switzerland) · 2020Review
- Pretreatment of Lignocellulosic Materials as Substrates for Fermentation Processes.Molecules (Basel, Switzerland) · 2018Review
- Combined strategy of transcription factor manipulation and β-glucosidase gene overexpression in Trichoderma reesei and its application in lignocellulose bioconversion.Journal of industrial microbiology & biotechnology · 2018Article
- Advantages of a distant cellulase catalytic base.The Journal of biological chemistry · 2018Article
- Intein-mediated assembly of tunable scaffoldins for facile synthesis of designer cellulosomes.Applied microbiology and biotechnology · 2018Article
- Production of highly efficient cellulase mixtures by genetically exploiting the potentials of Trichoderma reesei endogenous cellulases for hydrolysis of corncob residues.Microbial cell factories · 2017Article
- Genetics, Molecular, and Proteomics Advances in Filamentous Fungi.Current microbiology · 2017Review
- Conferring cellulose-degrading ability toBiotechnology for biofuels · 2017Article
- Single-molecule Imaging Analysis of Binding, Processive Movement, and Dissociation of Cellobiohydrolase Trichoderma reesei Cel6A and Its Domains on Crystalline Cellulose.The Journal of biological chemistry · 2016Article
- A Structurally Novel Chitinase from the Chitin-Degrading Hyperthermophilic Archaeon Thermococcus chitonophagus.Applied and environmental microbiology · 2016Article
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5 authors.
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Abstract
Dispersed cellulose ribbons from bacterial cellulose were subjected to digestion with cloned Cel7A (cellobiohydrolase [CBH] I) and Cel6A (CBH II) from Humicola insolens either alone or in a mixture and in the presence of an excess of beta-glucosidase. Both Cel7A and Cel6A were effective in partially converting the ribbons into soluble sugars, Cel7A being more active than Cel6A. In combination, these enzymes showed substantial synergy culminating with a molar ratio of approximately two-thirds Cel6A and one-third Cel7A. Ultrastructural transmission electron microscopy (TEM) observations indicated that Cel7A induced a thinning of the cellulose ribbons, whereas Cel6A cut the ribbons into shorter elements, indicating an endo type of action. These observations, together with the examination of the digestion kinetics, indicate that Cel6A can be classified as an endo-processive enzyme, whereas Cel7A is essentially a processive enzyme. Thus, the synergy resulting from the mixing of Cel6A and Cel7A can be explained by the partial endo character of Cel6A. A preparation of bacterial cellulose ribbons appears to be an appropriate substrate, superior to Valonia or bacterial cellulose microcrystals, to visualize directly by TEM the endo-processivity of an enzyme such as Cel6A.
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