The Canadian Journal of Chemical Engineering

Volume 71, Issue 6 pp. 917-924

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The effect of oxygen upon the kinetics of glucose oxidase inactivation

Ramakrishnan Venugopal,

Ramakrishnan Venugopal

Department of Chemical Engineering and Applied Chemistry, University of Toronto, Toronto, Ontario, Canada M5S lA4

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Bradley A. Saviue,

Corresponding Author

Bradley A. Saviue

Department of Chemical Engineering and Applied Chemistry, University of Toronto, Toronto, Ontario, Canada M5S lA4

Department of Chemical Engineering and Applied Chemistry, University of Toronto, Toronto, Ontario, Canada M5S lA4Search for more papers by this author

Ramakrishnan Venugopal,

Ramakrishnan Venugopal

Department of Chemical Engineering and Applied Chemistry, University of Toronto, Toronto, Ontario, Canada M5S lA4

Search for more papers by this author

Bradley A. Saviue,

Corresponding Author

Bradley A. Saviue

Department of Chemical Engineering and Applied Chemistry, University of Toronto, Toronto, Ontario, Canada M5S lA4

Department of Chemical Engineering and Applied Chemistry, University of Toronto, Toronto, Ontario, Canada M5S lA4Search for more papers by this author

First published: December 1993

https://doi.org/10.1002/cjce.5450710613

Citations: 9

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Abstract

The effect of oxygen upon the inactivation rate of glucose oxidase was studied. Tests on enzyme stability during catalytic turnover were conducted under a range of oxygen partial pressures. A standard activity assay was used to monitor changes in glucose oxidase activity.

Studies revealed that oxygen influenced the inactivation of glucose oxidase. Inactivation rates during catalytic turnover ranged between 0.01143 +/- 0.0016 h^-1 under 10 kPa oxygen to 0.04879 +/- 0.0023 h^-1under 101 kPa oxygen. Statistically different inactivation rates were obtained at oxygen partial pressures of 10,15, 21, 51, and 76 kPa. The enzymatic turnover number decreased from 11.0 X 10⁴ to 5.7 X 10⁴when the oxygen partial pressure increased from 10 to 101 kPa, suggesting that enzyme utilization was most efficient at low oxygen partial pressures (<15 kPa).

Abstract

On a étudié l'effet de l'oxygène sur la vitesse d'inactivation de l'oxydase de glucose. Des essais ont été menés sur la stabilité des enzymes durant le cycle catalytique pour une game de pressions partielles de l'oxygène. Au moyen d'un essai d'activité standard, on a surveillé les changements survenant dans l'activité de l'oxydase glucose.

L'étude révèle que l'oxygène influence l'inactivation de l'oxydase glucose. Les vitesses d'inactivation durant le cycle catalytique varient entre 0,01143 +/- 0,0016 h^-1 à une pression d'oxygtne de 10 kPa et 0,04879 +/- 0,0023 h^-1 à une pression d'oxygèe de 101 kPa. Des vitesses d'inactivation statistiquement différentes ont été obtenues à des pressions d'oxygéne partielles de 10, 15, 21, 51 et 76 kPa. Le nombre de cycles enzymatiques diminue de 11,0 X 10⁴ à 5,7 x 10⁴ lorsque la pression d'oxygéne partielle augmente de 10 à 101 kPa, ce qui laisse croire que l'utilisation des enzymes a été plus efficace à de faibles pressions d'oxygène partielles (<15 kPa).

References

Agathos, S. N., and A. L. Demain, “ Optimization of Fermentation Processes Through the Control of in Vivo Inactivation of Microbial Biosynthetic Enzymes”, in “ Foundations and Thermodynamics of Biochemical Engineering”, H. W. Blanch, E. T. Papoutsakis, and G. Stephanopoulos, Eds., ACS Symp. Ser 207, American Chemical Society, Washington, D.C., (1983), pp. 53–67.
10.1021/bk-1983-0207.ch003
Web of Science® Google Scholar
Altomare, R. E., J. Kohler, P. F. Greenfield, and J. R. Kittrell, “Deactivation of Immobilized Beef Liver Catalase by Hydrogen Peroxide”, Biotech. Bioeng. 16, 1659–1673 (1974).
10.1002/bit.260161208
CAS PubMed Web of Science® Google Scholar
Buchholz, K. and B. Godelmann, “Macrokinetics and Operational Stability of Immobilized Glucose Oxidase and Catalase”, Biotech. Bioeng. 20, 1201–1220 (1978).
10.1002/bit.260200807
CAS Web of Science® Google Scholar
Canovas, F., J. Tudela, C. Madrid, R. Varon, F. Carmona, and J. Lozano, “Kinetic Study on the Suicide Inactivation of Tyrosinase Induced by Catechol”, Biochim. Biophys. Acta 912, 417–423 (1987).
10.1016/0167-4838(87)90047-1
PubMed Web of Science® Google Scholar
Dawson, C. R. and K. Tokuyama, “On the Inactivation of Ascorbic Acid Oxidase”, Ann. N.Y. Acad. Sci. 92, 212–222 (1961).
10.1111/j.1749-6632.1961.tb46121.x
CAS PubMed Web of Science® Google Scholar
Demain, A. L. and S. N. Agathos, “Studies on in vivo Inactivation of Gramicidin S Synthetase and its Retardation”, Can. J. Microbiol. 32, 208–214 (1986).
10.1139/m86-042
CAS PubMed Web of Science® Google Scholar
Dietler, C. and K. Lerch, “ Reaction Inactivation of Tyrosinase”, in “ Oxidases and Related Redox Systems”, T. E. King, H. S. Mason, and M. Morrison, Eds, Pergamon, Oxford, (1982), pp. 305–317.
10.1016/B978-0-08-024421-1.50019-7
Google Scholar
Do, D. D. and R. H. Weiland, “Consistency Between Rate Expressions for Enzyme Reactions and Inactivation”, Biotech. Bioeng. 22, 1087–1093 (1980).
10.1002/bit.260220515
CAS Web of Science® Google Scholar
Dyrkacz, G. R., R. D. Libby, and G. A. Hamilton, “Trivalent Copper as a Probable Intermediate in the Reaction Catalyzed by Galactose Oxidase”, J. Am. Chem. Soc. 98, 626–628 (1976).
10.1021/ja00418a060
CAS PubMed Web of Science® Google Scholar
Greenfield, P. F., J. R. Kittrell, and R. L. Laurence, “Inactivation of Glucose Oxidase by Hydrogen Peroxide”, Anal. Biochem. 65, 109–124 (1975).
10.1016/0003-2697(75)90497-2
CAS PubMed Web of Science® Google Scholar
Gibson, Q. H., B. E. P. Swoboda and V. Massey, “Kinetics and Mechanism of Action of Glucose Oxidase”, J. Biol. Chem. 239, 3927–3934 (1964).
10.1016/S0021-9258(18)91224-X
CAS PubMed Web of Science® Google Scholar
Ivanetich, K. M., M. Ziman, and J. J. Bradshaw, “Reaction Schemes for the Degradation of Cytochrome P-450 by Allylisopropyl-acetamide and Fluroxene”, Biochem. Pharmacol. 29, 2808–2811 (1980).
10.1016/0006-2952(80)90015-5
Web of Science® Google Scholar
Kost, J., T. A. Horbett, B. D. Ratner, and M. Singh, “Glucose-Sensitive Membranes Containing Glucose Oxidase: Activity, Swelling, and Permeability Studies”, J. Biomed. Matl. Res. 19, 1117–1133 (1985).
10.1002/jbm.820190920
CAS PubMed Web of Science® Google Scholar
Krishnaswamy, S. and J. R. Kittrell, “Deactivation Studies of Immobilized Glucose Oxidase”, Biotech. Bioeng. 20, 821–835 (1978).
10.1002/bit.260200605
CAS Web of Science® Google Scholar
Levine, R. L., C. N. Oliver, R. M. Fulks, and E. R. Stadtman, “Turnover of Bacterial Glutamine Synthetase: Oxidative Inactivation Precedes Proteolysis”, Proc. Natl. Acad. Sci. USA 78, 2120–2124 (1981).
10.1073/pnas.78.4.2120
CAS PubMed Web of Science® Google Scholar
Nakamura, S. and Y. Ogura, “Action Mechanism of Glucose Oxidase of Aspergillus niger”, J. Biochem. 63 (3), 308–316 (1968).
CAS PubMed Web of Science® Google Scholar
Saville, B. A., M. R. Gray, and Y. K. Tam, “Evidence for Lidocaine-Induced Enzyme Inactivation”, J. Pharm. Sci. 78 (12), 1003–1008 (1989).
10.1002/jps.2600781207
CAS PubMed Web of Science® Google Scholar
Saville, B. A., and S. Persi, “The Effect of Oxygen Upon the Kinetics of Enzyme Inactivation: In Vitro Investigations Using Glutamine Synthetase”, Can. J. Chem. Eng. 70, 1143–1148 (1992).
10.1002/cjce.5450700614
CAS Web of Science® Google Scholar
Weibel, K. M. and H. J. Bright, “The Glucose Oxidase Mechanism”, J. Biol. Chem. 246, 2734–2744 (1971).
CAS PubMed Web of Science® Google Scholar

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Volume71, Issue6

December 1993

Pages 917-924

The effect of oxygen upon the kinetics of glucose oxidase inactivation

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The effect of oxygen upon the kinetics of glucose oxidase inactivation

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