Intrinsic kinetic constants of an immobilised glucose‐isomerase

M. D. Benaiges; C. Solà; C. De Mas

doi:10.1002/jctb.280361008

Intrinsic kinetic constants of an immobilised glucose‐isomerase

M. D. Benaiges, C. Solà, C. De Mas

Department of Chemistry

Research output: Contribution to journal › Article › Research › peer-review

13 Citations (Scopus)

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	https://doi.org/10.1002/jctb.280361008
Publication status	Published - 1 Jan 1986

Keywords

Bacillus coagulans
fructose syrup
glucose isomerase
immobilised enzymes
kinetics
mass transfer effects

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title = "Intrinsic kinetic constants of an immobilised glucose‐isomerase",

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 {\textcopyright} 1986 Society of Chemical Industry",

keywords = "Bacillus coagulans, fructose syrup, glucose isomerase, immobilised enzymes, kinetics, mass transfer effects",

author = "Benaiges, {M. D.} and C. Sol{\`a} and {De Mas}, C.",

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T1 - Intrinsic kinetic constants of an immobilised glucose‐isomerase

AU - Benaiges, M. D.

AU - Solà, C.

AU - De Mas, C.

PY - 1986/1/1

Y1 - 1986/1/1

N2 - 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

AB - 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

KW - Bacillus coagulans

KW - fructose syrup

KW - glucose isomerase

KW - immobilised enzymes

KW - kinetics

KW - mass transfer effects

U2 - 10.1002/jctb.280361008

DO - 10.1002/jctb.280361008

M3 - Article

VL - 36

SP - 480

EP - 486

IS - 10

ER -