Abstract
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. Copyright © 1986 Society of Chemical Industry
| Original language | English |
|---|---|
| Pages (from-to) | 480-486 |
| Journal | Journal of Chemical Technology & Biotechnology |
| Volume | 36 |
| Issue number | 10 |
| DOIs | |
| Publication status | Published - 1 Jan 1986 |
Keywords
- Bacillus coagulans
- fructose syrup
- glucose isomerase
- immobilised enzymes
- kinetics
- mass transfer effects
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Benaiges, M. D., Solà, C., & De Mas, C. (1986). Intrinsic kinetic constants of an immobilised glucose‐isomerase. Journal of Chemical Technology & Biotechnology, 36(10), 480-486. https://doi.org/10.1002/jctb.280361008