Any feedback?
Literature summary for 3.2.1.91 extracted from
- Isotherms for adsorption of cellobiohydrolase 1 and II from trichoderma reesei on microcrystalline cellulose (1997), Appl. Biochem. Biotechnol., 66, 39-56 .
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Trichoderma reesei | P07987 | - |
- |
| Trichoderma reesei | P62694 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Trichoderma reesei |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| CBH I | - |
Trichoderma reesei |
| CBH II | - |
Trichoderma reesei |
| cellobiohydrolase I | - |
Trichoderma reesei |
| cellobiohydrolase II | - |
Trichoderma reesei |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | study of adsorption to microcrystalline cellulose (Avicel) of pure cellobiohydrolase I from Trichoderma reesei. Adsorption isotherms of the enzyme are measured. Several models (Langmuir, Freundlich, Temkin, Jovanovic) are tested to describe the experimental adsorption isotherms. The isotherms do not follow the basic (one site) Langmuir equation. The experimental isotherms are best described by a model of Langmuir type with two adsorption sites and by a combined Langmuir-Freundlich model (analogous to the Hill equation). The isotherms when analyzed with the combined Langmuir-Freundlich model indicated presence of unequal binding sites on cellulose and/or negative cooperativity in the binding of the enzyme molecules | Trichoderma reesei |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
