Solute modulation of urease inactivation kinetics

Enzyme and Microbial Technology

Volumn 19, Issue 3, 1996, Pages 232-237

  Lencki, Robert W ^a,b   Neufeld, Ronald J ^a  

^a MCGILL UNIVERSITY   (Canada)

^b UNIVERSITY OF GUELPH   (Canada)

Author keywords

Aggregation; Dissociation; Inactivation; Salts; Solvents; Urease

Indexed keywords

AGGLOMERATION; DISSOCIATION; METHANOL; REACTION KINETICS; SALTS; SODIUM COMPOUNDS; SOLVENTS;

GLYCEROLS; HOFMEISTER SERIES; HYDROPHOBIC FORCE; RATE LIMITING STEP; SODIUM SULFATE; SOLUTE MODULATION; UREASE INACTIVATION;

ENZYME KINETICS;

ACETONE; GLYCEROL; INORGANIC SALT; LITHIUM CHLORIDE; METHANOL; POTASSIUM NITRATE; SODIUM SULFATE; SOLVENT; UREASE;

ARTICLE; CONTROLLED STUDY; ENZYME INACTIVATION; ENZYME KINETICS; PROTEIN QUATERNARY STRUCTURE; REACTION ANALYSIS;

EID: 0030586919     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/0141-0229(95)00226-X     Document Type: Article

References (25)

1. 1. Scopes, R. K. Protein Purification. Springer-Verlag, New York, 1987, 41-185
2. 2. Fukui, S. and Tanaka, A. Application of biocatalysts immobilized by prepolymer methods. Adv. Biochem. Eng. Biotechnol. 1984, 29, 2-33
3. 3. Schulze, B. and Klibanov, A. M. Inactivation and stabilization of subtilisins in neat organic solvents. Biotechnol. Bioeng. 1991, 38, 1001-1006
4. 2. Biotechnol. Bioeng. 1992, 39, 273-280
5. 5. Herskovits, T. T. and Jaillet, H. Structural stability and solvent denaturation of myoglobin. Science 1969, 163, 282-285
6. 6. von Hippel, P. H. and Wong, K.-Y. Neutral salts: The generality of their effects on the stability of macromolecular conformations. Science 1964, 145, 577-580
7. 7. von Hippel, P. H. and Schleich, T. The effect of neutral salts on the structure and conformational stability of macromolecules in solution. Biol. Macromol. 1969, 2, 417-573
8. 8. Asakura, T., Adachi, K., and Schwartz, E. Stabilizing effect of various organic solvents on protein. J. Biol. Chem. 1978, 18, 6423-6425
9. 9. Ye, W. N., Combes, D., and Monsan, P. Influence of additives on the thermostability of glucose oxidase. Enzyme Microb. Technol. 1988, 10, 498-502
10. 10. Gekko, K. and Timasheff, S. N. Mechanism of protein stabilization by glycerol: Preferential hydration in glycerol-water mixtures. Biochemistry 1981, 20, 4667-4676
11. 11. Lee, J. C. and Timasheff, S. N. The stabilization of proteins by sucrose. J. Biol. Chem. 1981, 256, 7193-7201
12. 12. Lencki, R. W., Arul, J., and Neufeld, R. J. Effect of subunit dissociation, denaturation, aggregation, coagulation, and decomposition on enzyme inactivation kinetics: I. First-order behavior. Biotechnol. Bioeng. 1992, 40, 1421-1426
13. 13. Lencki, R. W., 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
14. 14. Contaxis, C. C. and Reithel, F. J. Studies on protein multimers. II. A study of the mechanism of urease dissociation in 1,2-propanediol: Comparative studies with ethylene glycol and glycerol. J. Biol. Chem. 1971, 246, 677-685
15. 15. Fishbein, W. N., Nagarajan, K., and Scurzi, W. Urease catalysis and structure. IX. The half-unit and hemipolymers of jack bean urease. J. Biol. Chem. 1973, 248, 7870-7877
16. 16. Blakeley, R. L., Webb, E. C., and Zerner, B. Jack bean urease (E.C. 3.5.1.5). A new purification and reliable rate assay. Biochemistry 1969, 8, 1984-1990
17. 17. Huang, T.-C. and Chen, D. -H. Kinetic study of urease-catalyzed urea hydrolysis. J. Chem. Tech. Biotechnol. 1991, 52, 433-444
18. 18. Weatherburn, M. W. Phenol-hypochlorite reaction for determination of ammonia. Anal. Chem. 1969, 39, 971-974
19. 19. Castellan, G. W. Physical Chemistry. Addison-Wesley, Reading, MA, 1971, 780-789
20. 20. Brandts, J. F. Conformational transitions of proteins in water and in aqueous mixtures. Biol. Macromol. 1969, 2, 213-290
21. 21. Edsall, J. T. and Wyman, J. Biophysical Chemistry Vol. 1. Academic Press, New York, 1958, 282-322
22. 22. Secenov, I. M. Ueber die konstitution der salzlösungen auf grund ihres verhaltens zu kohlensäure. Z. Phys. Chem. 1889, 4, 117-125
23. 23. Franks, F. The hydrophobic interaction. In: Water: A Comprehensive Treatise Vol. 4 (Franks, F., Ed.). Plenum, New York, 1975, 1-94
24. 24. Zettlmeissl, G., Rudolph, R., and Jaenicke, R. Reconstitution of lactic dehydrogenase. Noncovalent aggregation vs. reactivation. 1. Physical properties and kinetics of aggregation. Biochemistry 1979, 18, 5567-5571
25. 25. Lencki, R. W., Tecante, A., and Choplin, L. Effect of shear on the inactivation of the enzyme dextransucrase. Biotechnol. Bioeng. 1993, 42, 1061-1067