Influence of immobilization on the thermal inactivation of yeast invertase

Enzyme and Microbial Technology

Volumn 21, Issue 3, 1997, Pages 196-202

  Vrábel, Peter ^a   Polakovič, Milan ^a   Godó, Štefan ^a   Báleš, Vladimír ^a   Dočolomanský, Peter ^b   Gemeiner, Peter ^c  

^a SLOVAK UNIVERSITY OF TECHNOLOGY   (Slovakia)

^b INSTITUTE OF MOLECULAR PHYSIOLOGY AND GENETICS   (Slovakia)

^c INSTITUTE OF CHEMISTRY   (Slovakia)

Author keywords

Activated cellulose; Concanavalin A; Enzyme inactivation; Glutaraldehyde cross linking; Immobilization; Inactivation kinetics; Invertase; Mechanism analysis; Multitemperature evaluation

Indexed keywords

ACTIVATION ENERGY; ADSORPTION; ALDEHYDES; CATALYST ACTIVITY; CELLULOSE; CROSSLINKING; MATHEMATICAL MODELS; REACTION KINETICS; THERMODYNAMIC STABILITY; YEAST;

CONCANAVALIN; ENZYME INACTIVATION; GLUTARALDEHYDE; INVERTASE; MULTITEMPERATURE EVALUATION;

ENZYME IMMOBILIZATION;

BETA FRUCTOFURANOSIDASE; CELLULOSE; CONCANAVALIN A; GLUTARALDEHYDE;

ADSORPTION; ARTICLE; CROSS LINKING; ENZYME ACTIVITY; ENZYME IMMOBILIZATION; ENZYME INACTIVATION; ENZYME KINETICS; INHIBITION KINETICS; NONHUMAN; THERMOSTABILITY; YEAST;

EID: 0037984516     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0141-0229(96)00266-9     Document Type: Article

References (22)

1. Mozhaev, V. V. and Martinek, K. Inactivation and reactivation of proteins (enzymes). Enzyme Microb. Technol. 1982, 4, 299-309
2. Edwards, R. A., Jacobson, A. L., and Huber, R. E. Thermal denaturation of β-galactosidase and two site-specific mutants. Bíochemistry 1990, 29, 11001-11008
3. Sugawara, T., Kuwajima, K., and Sugai, S. Folding of staphylococcal nuclease A studied by equilibrium and kinetic circular dichroism spectra. Biochemistry 1991, 30, 2698-2706
4. Zhang, Y. L., Zhou, J. M., and Tsou, C. L. Inactivation precedes conformation change during thermal denaturation of adenylate kinase. Biochim. Biophys. Acta 1993, 1164, 61-67
5. Porter, W. R., Staack, H., Brandt, K., and Manning, M. C. Thermal stability of low molecular weight urokinase during heat treatment. I. Effects of protein concentration, pH, and ionic strength. Thrombosis Res. 1993, 71, 265-279
6. Ikai, A. and Tanford, C. Kinetic evidence for incorrectly folded intermediate states in the refolding of denatured proteins. Nature 1971, 230, 100-102
7. Xiao, J., Liang, S. J., and Tsou, C. L. Inactivation before significant conformational change during denaturation of papain by guanidine hydrochloride. Biochim. Biophys. Acta 1993, 1164, 54-60
8. Privalov, P. L. Thermodynamic problems of protein structure. Ann. Rev. Biophys. Biophys. Chem. 1989, 18, 47-69
9. Chase, A. M. Studies on cell enzyme systems. IV. The kinetics of inactivation of Cypridina luciferase. J. Gen. Physiol. 1950, 33, 535-546
10. Henley, J. P. and Sadana, A. Series types enzyme deactivations: Influence of intermedíate activity on deactivation kinetics. Enzyme Microb. Technol. 1984, 6, 35-41
11. Gianfreda, L., Marruci, G., Grizzuti, N., and Greco, G. Series mechanism of enzyme deactivation. Characterization of intermediate forms. Biotechnol. Bioeng. 1985, 27, 877-882
12. Sadana, A. Biocatalysis. Fundamentals of Enzyme Deactivation Kinetics. Prentice Hall, Englewood Cliffs, NJ, 1991
13. Polakovič, M. and Vrábel, P. Analysis of the mechanism and kinetics of thermal inactivation of enzymes: Critical assessment of isothermal inactivation experiments. Process Biochem. 1996, 31, 787-800
14. Vrábel, P., Polakovič, M., Štefuca, V., and Báleš, V. Analysis of mechanism and kinetics of thermal inactivation of enzymes: Evaluation of multitemperature data applied to the inactivation of yeast invertase, Enzyme Microb. Technol., 1997, 20, 348-354
15. Martinek, K. and Mozhaev, V. Immobilization of enzymes: An approach to fundamental studies in biochemistry. Adv. Enzymol. 1985, 57, 179-249
16. Štefuca, V., Gemeiner, P., Kurillová, Ľ., Danielsson, B., and Báleš, V. Application of the enzyme thermistor to the direct estimation of intrinsic kinetics using the saccharose-immobilized invertase system. Enzyme Microb. Technol. 1990, 12, 830-835
17. Štefuca, V., Gemeiner, P., and Báleš, V. Study of porous cellulose beads as an enzyme carrier via simple mathematical models for the hydrolysis of saccharose using immobilized invertase reactors. Enzyme Microb. Technol. 1988, 10, 306-311
18. Dočolomanský, P., Gemeiner, P., Mislovičová, D., Štefuca, V., and Danielsson, B. Screening of concanavalin A-bead cellulose conjugates using an enzyme thermistor with immobilized invertase as the reporter catalyst. Biotechnol. Bioeng. 1994, 43, 286-292
19. Trinder, P. Determination of glucose in blood using glucose oxidase with an alternative oxygen receptor. Ann. Clin. Biochem. 1969, 6, 24-27
20. Kaszonyi, A. and Ilavský, J. A universal program for the calculation of the parameters of kinetic equations. Chem. Prum. 1988, 38/63, 660-661 (in Slovak)
21. Turková, J., Fusek, M., and Št'ovičková, J. Formation of biospecific complexes as a tool for oriented immobilization of enzymes. In: Interbiotech '87. Enzyme Technologies. Progress in Biotechnology Vol. 4 (Blažej, A. and Zemek, J., Ed.). Elsevier, Amsterdam, 1988, 245-260
22. Ahern, T. J. and Klibanov, A. M. The mechanism of irreversible enzyme inactivation at 100°C. Science 1985, 228, 1280-1284