Glucose Isomerase: A Case Study of Enzyme-Catalyzed Process Technology

Hamilton, Bruce K.; Colton, Clark K.; Cooney, Charles L.

doi:10.1007/978-1-4684-2088-3_7

Cited by 12 publications

(3 citation statements)

References 69 publications

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“…The activity recovery of immobilized glucose isomerase was 40-60%. This compares favorably with the typical recovery rates of less than 40% obtained by other immobilization methods [ 13]. We believe that this is largely due to the highly hydrophilic nature of fiber.…”

Section: Glucose Isomerasesupporting

confidence: 80%

A simple entrapment method for immobilizing enzymes within cellulose fibers

Linko¹,

Pohjola²,

Viskari

et al. 1976

FEBS Letters

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Section: Glucose Isomerasesupporting

confidence: 80%

A simple entrapment method for immobilizing enzymes within cellulose fibers

Linko¹,

Pohjola²,

Viskari

et al. 1976

FEBS Letters

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“…The glucose-fructose enzymatic isomerization can be described by the following mechanism (where G represents glucose, E the glucose isomerase enzyme, F fructose and X the intermediate complex) [1]:…”

Section: Inherent Kineticsmentioning

confidence: 99%

A study on intra-particle diffusion effects in enzymatic reactions: glucose-fructose isomerization

Giordano

Cooney

2000

Bioprocess Engineering

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In this work different aspects of the glucosefructose enzymatic isomerization, using immobilized glucose isomerase, are studied and quanti®ed. Reaction temperatures range from 40°C to 60°C. Intra-particle effective diffusivities (D e ), determined after uptake experiments, are between 1.20´10 )6 cm 2 /s, at 40°C, and 2.52´10 )6 cm 2 /s, at 60°C. The estimated energy of activation for diffusion (E aD ) is 7.71 kcal/mol. No signi®cant adsorption of the sugars on the support gel matrix is observed. Crushed particles (/ = 150±350 l) are used during kinetic experiments. For this range of particle diameters, inherent kinetics is approached. A reversible Michaelis± Menten rate equation is ®tted to the data, providing the following parameters at pH = 7.0: k 0 = 2.15´10 )6 g/IU/s; E a /R = 8998 K. Glucose (K G ) and fructose (K F ) af®nity constants are essentially the same, ranging from 0.190 M, at 40°C to 0.305 M, at 60°C. The thermodynamic equilibrium constant is determined for the three temperatures, and the heat of reaction, estimated from a Van't Hoff plot, is DH = 1682 cal/mol. Independent experiments, where the reaction occurs in the presence of signi®cant intra-particle mass transfer resistance, are used as validation tests.List of symbols C 0 Sugar concentration in the bulk of the solution, at the beginning of the uptake experiments, M D e Intra-particle (glucose and fructose) effective diffusivity, cm 2 /s D G Glucose molecular diffusion coef®cient in water, cm 2 /s E a Energy of activation of the isomerization reaction, cal/mol E aD Energy of activation of the intra-gel effective diffusivity, cal/mol E t enzymatic load, IU

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“…In these applications sucrose can be replaced by a mixture containing D-glucose and D-fructose, which can be obtained by isomerizing dextrose or corn starch hydrolyzates, which are less expensive and available in abundant supply in the United States. Hence the potential market for this type of mixture is enormous, and the enzymatic isomerization of D-glucose t o obtain a high-fructose liquid has come to attract the interest of every major corn-processing company as well as some sugar companies.2 In fact this industrial process represents one of the largest industrial applications of enzyme^.^ Much of the earlier work had been carried out in Japan, notably by Takasaki* and others, and for details one may refer to an extensive literature review by Hamilton et al 5 In spite of the importance of such potential applications and the extensiveness of literature, there has been very little quantitative work on reaction kinetics and enzyme deactivation.…”

Section: Introductionmentioning

confidence: 99%

A model for enzymatic isomerization of D‐glucose to D‐fructose in a batch reactor

Sproull

Lim

Schneider

1976

Biotech & Bioengineering

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Using whole cells containing glucose isomerase, mathematical models for the enzymatic conversion of D-glucose to D-fructose and for the inactivation of the enzyme catalyst have been postulated and verified experimentally. The heat of reaction, the equilibrium constant, and the individual rate constants and their activation energies have been estimated. The model can be used to predict the time course for the enzymatic production of fructose in a batch reactor within the tested experimental range of 40-80 degrees C.

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Glucose Isomerase: A Case Study of Enzyme-Catalyzed Process Technology

Cited by 12 publications

References 69 publications

A simple entrapment method for immobilizing enzymes within cellulose fibers

A simple entrapment method for immobilizing enzymes within cellulose fibers

A study on intra-particle diffusion effects in enzymatic reactions: glucose-fructose isomerization

A model for enzymatic isomerization of D‐glucose to D‐fructose in a batch reactor

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