ArticleAMB Express2014
Family 1 carbohydrate binding-modules enhance saccharification rates.
Article in AMB Express, 2014. 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, 37 citations in OpenAlex.
- The Role of Non-Catalytic Region in Determining the Difference in Efficiency Between Two Cellobiohydrolases Revealed Through a Genetic Approach.Journal of fungi (Basel, Switzerland) · 2025Article
- Metagenomic and Physicochemical Analyses Reveal Microbial Community and Functional Differences Between Three Different Grades of Hongxin Low-Temperature Daqu.Foods (Basel, Switzerland) · 2025Article
- Expression and Characterization of Two α-l-Arabinofuranosidases fromInternational journal of molecular sciences · 2023Article
- Unique properties of a Dictyostelium discoideum carbohydrate-binding module expand our understanding of CBM-ligand interactions.The Journal of biological chemistry · 2022Article
- Recombinant Family 1 Carbohydrate-Binding Modules Derived From Fungal Cellulase Enhance Enzymatic Degradation of Lignocellulose as Novel Effective Accessory Protein.Frontiers in microbiology · 2022Article
- Composition and biosynthetic machinery of theCell surface (Amsterdam, Netherlands) · 2019Article
- Article
- Controlled Aggregation and Increased Stability of β-Glucuronidase by Cellulose Binding Domain Fusion.PloS one · 2017Article
- Investigation of the binding properties of a multi-modular GH45 cellulase using bioinspired model assemblies.Biotechnology for biofuels · 2016Article
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
Cellulose degrading enzymes usually have a two-domain structure consisting of a catalytic domain and a non-catalytic carbohydrate-binding module. Although it is well known the importance of those modules in cell wall degrading process, their function is not yet fully understood. Here, we analyze the cellulose-hydrolysis activity enhancement promoted by the cellobiohydrolase I carbohydrate-binding module from Trichoderma harzianum. It was cloned, expressed, purified and used in combination with either a commercial cellulase preparation, T. reesei cellobiohydrolase I or its separate catalytic domain to hydrolyze filter paper. In all cases the amount of glucose released was increased, reaching up to 30% gain when the carbohydrate-binding module was added to the reaction. We also show that this effect seems to be mediated by a decrease in the recalcitrance of the cellulosic substrate. This effect was observed both for crystalline cellulose samples which underwent incubation with the CBM prior to application of cellulases and for the ones incubated simultaneously. Our studies demonstrate that family 1 carbohydrate-binding modules are able to potentiate the enzymatic degradation of the polysaccharides and their application might contribute to diminishing the currently prohibitive costs of the lignocellulose saccharification process.
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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.