Intrinsic kinetic constants of an immobilised glucose-isomerase
| Autor: | Carles Solà, Maria Dolors Benaiges, C. de Mas |
|---|---|
| Rok vydání: | 2007 |
| Předmět: |
Glucose-6-phosphate isomerase
Chromatography Immobilized enzyme Renewable Energy Sustainability and the Environment General Chemical Engineering Organic Chemistry Kinetics Inorganic chemistry chemistry.chemical_element Fructose Pollution Reversible reaction Inorganic Chemistry chemistry.chemical_compound Fuel Technology chemistry Mass transfer Waste Management and Disposal Cobalt Isomerization Biotechnology |
| Zdroj: | Scopus-Elsevier |
| ISSN: | 1097-4660 0268-2575 |
| DOI: | 10.1002/jctb.280361008 |
| Popis: | The isomerization of glucose into fructose using a commercial immobilised glucose-isomerase has been studied and an initial transitory state of the enzyme, probably due to an establishment of stationary concentration profiles, was observed. Operational conditions to minimise the effects of external and internal mass transfer were determined using immobilised enzyme particles with diameters less than 0.064 mm. Thermal enzyme deactivation of the enzyme was insignificant if it was pre-treated with cobalt. The intrinsic kinetic constants of the reversible reaction Michaelis—Menten equation were calculated, in operational conditions free of mass transfer effects. |
| Databáze: | OpenAIRE |
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