ArticleThe Biochemical journal2005
The interaction of carbohydrate-binding modules with insoluble non-crystalline cellulose is enthalpically driven.
Article in The Biochemical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 50 citations in OpenAlex.
- Isothermal Titration Calorimetry for Quantification of Protein-Carbohydrate Interactions.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Cellulose-specific Type B carbohydrate binding modules: understanding oligomeric and non-crystalline substrate recognition mechanisms.Biotechnology for biofuels · 2018Article
- Stability and Ligand Promiscuity of Type A Carbohydrate-binding Modules Are Illustrated by the Structure ofThe Journal of biological chemistry · 2017Article
- Complexity of the Ruminococcus flavefaciens cellulosome reflects an expansion in glycan recognition.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Recognition of xyloglucan by the crystalline cellulose-binding site of a family 3a carbohydrate-binding module.FEBS letters · 2015Article
- Family 46 Carbohydrate-binding Modules Contribute to the Enzymatic Hydrolysis of Xyloglucan and β-1,3-1,4-Glucans through Distinct Mechanisms.The Journal of biological chemistry · 2015Article
- Three-dimensional structural aspects of protein-polysaccharide interactions.International journal of molecular sciences · 2014Review
- Structural basis for entropy-driven cellulose binding by a type-A cellulose-binding module (CBM) and bacterial expansin.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- A coarse-grained model for synergistic action of multiple enzymes on cellulose.Biotechnology for biofuels · 2012Article
- Structural and mechanistic fundamentals for designing of cellulases.Computational and structural biotechnology journal · 2012Review
- Article
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1 author at 1 institution in 1 country.
Funding
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Abstract
Natural cellulose exists as a composite of cellulose forms, which can be broadly characterized as crystalline or non-crystalline. The recognition of both of these forms of cellulose by the CBMs (carbohydrate-binding modules) of microbial glycoside hydrolases is important for the efficient natural and biotechnological conversion of cellulosic biomass. The category of CBM that binds insoluble non-crystalline cellulose does so with an affinity approx. 10-20-fold greater than their affinity for cello-oligosaccharides and/or soluble polysaccharides. This phenomenon has been assumed to originate from the effects of changes in configurational entropy upon binding. The loss of configurational entropy is thought to be less profound upon binding to conformationally restrained insoluble non-crystalline cellulose, resulting in larger free energies of binding. However, using isothermal titration calorimetry, it is shown that this is not the case for the high-affinity interactions of CcCBM17 (the family 17 CBM from EngF of Clostridium cellulovorans) and BspCBM28 (the family 28 CBM from Cel5A of Bacillus species 1139) with regenerated cellulose, an insoluble preparation of primarily non-crystalline cellulose. The enhanced free energy of binding of non-crystalline cellulose relative to cello-oligosaccharides is by virtue of improved enthalpy, not entropy.
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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.