Analysis of mechanism and kinetics of thermal inactivation of enzymes: Evaluation of multitemperature data applied to inactivation of yeast invertase

Enzyme and Microbial Technology

Volumn 20, Issue 5, 1997, Pages 348-354

  Vrábel, Peter ^a   Polakovič, Milan ^a   Štefuca, Vladimír ^a   Báleš, Vladimír ^a  

^a SLOVAK UNIVERSITY OF TECHNOLOGY   (Slovakia)

Author keywords

Analysis of mechanism; Enzyme inactivation; Inactivation kinetics; Invertase; Multitemperature evaluation

Indexed keywords

DIFFERENTIAL EQUATIONS; ENZYME INHIBITION; MATHEMATICAL MODELS; REACTION KINETICS; THERMAL EFFECTS; YEAST;

ARRHENIUS EQUATION; YEAST INVERTASE;

ENZYMES;

BETA FRUCTOFURANOSIDASE;

ARTICLE; ENZYME INACTIVATION; ENZYME MECHANISM; METHODOLOGY; MOLECULAR MODEL; NONHUMAN; TEMPERATURE; TEMPERATURE DEPENDENCE; YEAST;

EID: 0342683812     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0141-0229(96)00150-0     Document Type: Article

References (34)

1. Hei, D. J. and Clark, D. S. Estimation of melting curves from enzymatic activity-temperature profiles. Biotechnol. Bioeng. 1993, 42, 1245-1251
2. Simon, L. M., Kotormán, M., Szajáni, B., and Boross, L. Preparation and characterization of immobilized glucose-phosphate isomerase. Enzyme Microb. Technol. 1986, 8, 222-226
3. Erarslan, A., and Kocer, H. Thermal inactivation kinetics of penicillin G acylase obtained from a mutant derivative of Escherichia coli ATCC 11105. J. Chem. Technol. Biotechnol. 1992, 55, 79-84
4. Wright, G. G. and Schomaker, V. Studies on the denaturation of antibody. III. Kinetic aspects of the inactivation of diphtheria anti-toxin by urea. J. Am. Chem. Soc. 1948, 70, 356-364
5. Chase, A. M. Studies on cell enzyme systems. IV. The kinetics of inactivation of Cypridina luciferase. J. Gen. Physiol. 1950, 33, 535-546
6. Gianfreda, L., Marruci, G., Grizzuti, N., and Greco, G. Acid phosphatase deactivation by a series mechanism. Biotechnol. Bioeng. 1984, 26, 518-527
7. Gianfreda, L., Marruci, G., Grizzuti, N., and Greco, G. Series mechanism of enzyme deactivation. Characterization of intermediate forms. Biotechnol. Bioeng. 1985, 27, 877-882
8. Mansfeld, J. and Schellenberger, A. Investigation of thermal stability of immobilized invertase. Acta Biotechnol. 1986, 6, 89-99 (in German)
9. Ulbrich, R., Schellenberger, A., and Damerau, W. Studies on the thermal inactivation of immobilized enzymes. Biotechnol. Bioeng. 1986, 28, 511-522
10. Siksnis, V., Mozhaev, V. V., Galkantaite, N., Melik-Nubarov, N. S., Denis, G., and Martinek, K. Unusual (zig-zag) temperature dependence of the rate constant for irreversible thermoinactivation of hydrophilized enzymes. Collect. Czech. Chem. Commun. 1990, 55, 1366-1371
11. Greco, G., Pirozzi, D., and Gianfreda, L. Thermal equivalence criteria in the chemical deactivation and stabilization of acid phosphatase. Enzyme Microb. Technol. 1991, 13, 353-358
12. Gianfreda, L., Toscano, G., Pirozzi, D., and Greco, G. The effect of sorbitol on acid phosphatase deactivation. Biotechnol. Bioeng. 1991, 38, 1153-1158
13. Yoshioka, S., Izutsu, K., Aso, Y., and Takeda, Y. Inactivation kinetics of enzyme pharmaceuticals in aqueous solution. Pharm. Res. 1991, 8, 480-484
14. Mozhaev, V. V., S., Melik-Nubarov, N.S., Levitsky, V. Y., Siksnis, V. A., and Martinek, K. High stability to irreversible inactivation at elevated temperatures of enzymes covalently modified by hydrophilic reagents: α-chymotrypsin. Biotechnol. Bioeng. 1992, 40, 650-662
15. Lencki, W. R., Arul, J., and Neufeld, R. J. Effect of subunit dissociation, denaturation, aggregation, coagulation, and decomposition on enzyme inactivation kinetics. II. Biphasic and grace period behavior. Biotechnol. Bioeng. 1992, 40, 1427-1434
16. Owusu, R. K. and Berthalon, N. A test for the two-stage thermoinactivation model for chymotrypsin. Food Chem. 1993, 48, 231-235
17. Nohara, D., Yamada, T., Watanabe, A., and Sakai, T. Equilibrium and kinetic studies on reversible and irreversible denaturation of micrococcal nuclease. Biotechnol. Bioeng. 1994, 44, 276-282
18. Greco, G. and Gianfreda, L. An experimental technique for the discrimination between series and parallel mechanisms of enzyme deactivation. Biotechnol. Lett. 1984, 6, 693-697
19. Toscano, G., Pirozzi, D., Maremonti, M., Gianfreda, L., and Greco, G. Kinetics of enzyme deactivation: A case study. Catal Today 1994, 22, 489-510
20. Polakovič, M. and Vrábel, P. Analysis of mechanism and kinetics of thermal inactivation of enzymes: Critical assessment of isothermal inactivation experiments. Process Biochem., 1996, 37, 787-800
21. Schülke, N. and Schmidt, F. X. The stability of yeast invertase is not significantly influenced by glycosylation. J. Biol. Chem. 1988, 263, 8827-8831
22. Kern, G., Schülke, N., Schmid, F. X., and Jaenicke, R. Stability, quaternary structure, and folding of internal, external, and core-glycosylated invertase from yeast. Protein Sci. 1992, 1, 120-131
23. Trimble, R. B. and Maley, F. Subunit structure of external invertase from Saccharomyces cerevisiae. J. Biol Chem. 1977, 252, 4409-4412
24. Chu, F. K., Watorek, W., and Maley, F. Factors affecting the oligomeric structure of yeast external invertase. Arch. Biochem. Biophys. 1983, 223, 543-555
25. Esmon, P. C., Esmon, B. E., Schauer, I. E., Taylor, A., and Schekman, R. Structure, assembly, and secretion of octameric invertase. J. Biol. Chem. 1987, 262, 4387-4394
26. Reddy, A. V., MacColl, R., and Maley, F. Effect of oligosaccharides on oligomeric structures of external, internal, and deglycosylated invertase. Biochemistry 1990, 29, 2482-2487
27. Kittrell, J. R. Modeling of chemical reactions. In: Advances in Chemical Engineering Vol. 8 (Drew, T. B., Cokelet, G. R., Hoopes, J. W., and Vermeulen, T., Eds.). Academic Press, New York, 1970, 97-184
28. Štefuca, V., Gemeiner, P., Kurillová, L'., 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
29. Trinder, P. Determination of glucose in blood using glucose oxidase with an alternative oxygen receptor. Ann. Clin. Biochem. 1969, 6, 24-27
30. Lowry, O. H., Rosebrough, N. J., Farr, A. L., and Randall, R. J. Protein measurement with the Folin phenol reagent. J. Biol. Chem. 1951, 193, 265-275
31. Kaszonyi, A. and Ilavský, J. A universal program for the calculation of the parameters of kinetic equations. Chem. Prům. 1988, 38/63, 660-661 (in Slovak)
32. Vrábel, P. Investigation of the deactivation kinetics of yeast invertase. Dipl. Eng. thesis, Slovak Technical University, Bratislava, Slovakia, 1991 (in Slovak)
33. Ooshima, H., Sakimoto, M., and Harano, Y. Kinetic study on thermal stability of immobilized invertase. Biotechnol. Bioeng. 1980, 22, 2169-2178
34. Schülke, N. and Schmidt, F. X. Effect of glycosylation on the mechanism of renaturation of invertase from yeast. J. Biol. Chem. 1988, 263, 8832-8837