Homologous xylanases from Clostridium thermocellum: evidence for bi-functional activity, synergism between xylanase catalytic modules and the presence of xylan-binding domains in enzyme complexes. [electronic resource]
Producer: 19991020Description: 105-10 p. digitalISSN:- 0264-6021
- Acetylation
- Amidohydrolases -- chemistry
- Bacterial Proteins -- chemistry
- Binding Sites
- Catalytic Domain
- Cellulose -- analogs & derivatives
- Cloning, Molecular
- Clostridium -- enzymology
- Enzyme Stability
- Genes, Bacterial -- genetics
- Hydrogen-Ion Concentration
- Hydrolysis
- Kinetics
- Ligands
- Multienzyme Complexes -- chemistry
- Sequence Deletion
- Sequence Homology, Amino Acid
- Solubility
- Substrate Specificity
- Temperature
- Xylan Endo-1,3-beta-Xylosidase
- Xylans -- metabolism
- Xylosidases -- chemistry
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Publication Type: Journal Article; Research Support, Non-U.S. Gov't
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