Intrinsic kinetic constants of an immobilised glucose‐isomerase

M. D. Benaiges, C. Solà, C. De Mas

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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 languageEnglish
Pages (from-to)480-486
JournalJournal of Chemical Technology & Biotechnology
Volume36
Issue number10
DOIs
Publication statusPublished - 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