Studies on the properties of Celluclast/Eudragit L-100 conjugate
| Autor: | Fernando Dourado, Francisco M. Gama, Maria de Lurdes Bastos, Manuel Mota |
|---|---|
| Přispěvatelé: | Universidade do Minho |
| Jazyk: | angličtina |
| Rok vydání: | 2002 |
| Předmět: |
0106 biological sciences
Immobilized enzyme Bioengineering Cellulase 01 natural sciences Applied Microbiology and Biotechnology Sensitivity and Specificity DSC 03 medical and health sciences chemistry.chemical_compound Carbodiimide Adsorption Polymethacrylic Acids 010608 biotechnology Enzyme Stability Enzyme immobilization Denaturation (biochemistry) Solubility Trichoderma reesei 030304 developmental biology chemistry.chemical_classification Trichoderma 0303 health sciences Chromatography Science & Technology biology Chemistry Eudragit L-100 General Medicine Polymer Hydrogen-Ion Concentration biology.organism_classification Enzymes Immobilized Chemical engineering biology.protein Biotechnology |
| Zdroj: | Repositório Científico de Acesso Aberto de Portugal Repositório Científico de Acesso Aberto de Portugal (RCAAP) instacron:RCAAP |
| Popis: | A cellulase from Trichoderma reesei was immobilized on Eudragit L-100, a reversibly soluble polymer depending on the pH of the medium. The solubility of the modified cellulase was studied at different pH values. By changing the pH, the adsorption equilibrium of the derivatized proteins is switched towards the liquid phase, thus making recycling possible. This method allows for improved stability, without major loss of specific activity. The adsorption of cellulase on Eudragit lowers the enthalpy of denaturation, but affects only slightly the denaturation temperature. The use of carbodiimide was ineffective on linking the enzymes covalently to the polymer, since the immobilization process was found to be only mediated by non-covalent forces. INCO-DC (96-2205) - OLONOCO. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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