pH control of the catalytic activity of cross-linked enzyme crystals in organic solvents

Journal of the American Chemical Society

Volumn 118, Issue 41, 1996, Pages 9815-9819

  Xu, Kui ^a   Klibanov, Alexander M ^a  

^a MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

SUBTILISIN;

ARTICLE; ENZYME ACTIVITY; ENZYME STRUCTURE; PH; PROTEIN CROSS LINKING; SOLUBILIZATION;

EID: 0029858946     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja961596m     Document Type: Article

References (46)

1. (a) St. Clair, N. L.; Navia, M. A. J. Am. Chem. Soc. 1992, 114, 7314.
2. (b) Sobolov, S. B.; Bartoszko-Malik, A.; Oeschger, T. R.; Montelbano, M. M. Tetrahedron Lett. 1994, 35, 7751.
3. (c) Persichetti, R. A.; St. Clair, N. L.; Griffith, J. P.; Navia, M. A.; Margolin, A. L. J. Am. Chem. Soc. 1995, 117, 2732.
4. (d) Lalonde, J. J.; Govardhan, C.; Khalaf, N.; Martinez, A. G.; Visuri, K.; Margolin, A. L. J. Am. Chem. Soc. 1995, 117, 6845.
5. (e) Sobolov, S. B.; Leonida, M. D.; Bartoszko-Malik, A.: Voivodov, K. I.; McKinney, F.; Kim, J.; Fry, A. J. J. Org. Chem. 1996, 61, 2125.
6. (f) Khalaf, N.; Govardhan, C. P.; Lalonde, J. J.; Persichetti, R. A.; Wang, Y.-F.; Margolin, A. L. J. Am. Chem. Soc. 1996, 118, 5494.
7. (a) Schmitke, J. L.; Wescott, C. R.; Klibanov, A. M. J. Am. Chem. Soc. 1996, 118, 3360.
8. (b) Ke. T.; Wescott, C. R.; Klibanov, A. M. J. Am. Chem. Soc. 1996, 118, 3366.
9. (a) Fitzpatrick, P. A.; Steinmetz, A. C. U.; Ringe, D.; Klibanov, A. M. Proc. Natl. Acad. Sci. U.S.A. 1993, 90, 8653.
10. (b) Fitzpatrick, P. A.; Ringe, D.; Klibanov, A. M. Biochem. Biophys. Res. Commun. 1994, 198, 675.
11. (c) Yennawar, N. H.; Yennawar, H. P.; Farber, G. K. Biochemistry 1994, 33, 7326.
12. (d) Yennawar, H. P.; Yennawar, N. H.; Farber, G. K. J. Am. Chem. Soc. 1995, 117, 577.
13. (a) Klibanov, A. M. Trends Biochem. Sci. 1989, 14, 141.
14. (b) Chen, C.-S.; Sih, C. J. Angew. Chem., Int. Ed. Engl. 1989, 28, 695.
15. (c) Dordick, J. S. Enzyme Microb. Technol. 1989, 11, 194.
16. (d) Klibanov, A. M. Acc. Chem. Res. 1990, 23, 114.
17. (e) Gupta, M. N. Eur. J. Biochem. 1992, 203, 25.
18. (f) Faber, K.; Riva, S. Synthesis 1992, 895.
19. (g) Hailing, P. J. Ertzyme Microb. Technol. 1994, 16, 178.
20. (h) Koskinen, A. M. P., Klibanov, A. M., Eds. Enzymatic Reactions in Organic Media; Blackie: London. 1996.
21. (a) Dong, A.; Prestrelski, S. J.; Allison, S. D.; Carpenter, J. F. J. Pharm. Sci. 1995, 84, 415.
22. (b) Griebenow, K.; Klibanov, A. M. Proc. Natl. Acad. Sci. U.S.A. 1995, 92. 10969.
23. Fersht, A. Enzyme Structure and Mechanism, 2nd ed.; Freeman: New York, 1985; Chapter 5.
24. Bates, R. G. Determination of pH. Theory and Practice, 2nd ed.; Wiley: New York, 1964; Chapters 7 and 8.
25. (a) Zaks, A.; Klibanov, A. M. Proc. Natl. Acad. Sci. U.S.A. 1985, 82, 3192.
26. (b) Zaks, A.; Klibanov, A. M. J. Biol. Chem. 1988, 263, 3194.
27. Yang, Z.; Zacherl, D.; Russell, A. J. J. Am. Chem. Soc. 1993, 115, 12251.
28. Blackwood, A. D.; Curran, L. J.; Moore, B. D.; Hailing, P. J. Biochim. Biophys. Acta 1994, 1206, 161. An organic-phase buffer is an appropriate mixture of a Brønsted-Lowry acid and its conjugate base which can control the protonation state of other ionogenic compounds present in the same organic solvent.
29. a decreasing when the activity of water increases.
30. We also attempted a complimentary test, whereby subtilisin CLCs were lyophilized from 20 mM aqueous phosphate buffer solutions of pH 5 and 11 to determine whether this procedure would give rise to the pH memory. However, it was found that both resultant preparations were at least 1 order of magnitude less active than the original CLCs, presumably due to a collapse of the crystal and a consequent blockage of enzyme molecules in its interior. These observations made this particular test equivocal.
31. 2a). The thermodynamic water activity of 0.85 was maintained in the rest of this work.
32. For a review, see: Philipp, M.; Bender, M. L. Mol. Cell. Biochem. 1983, 51, 5.
33. Ochiai, K.; Seto, K. J. Nucl. Sci. Technol. 1971, 8, 330.
34. Krasovec, F. Croat. Chem. Acta 1965, 37, 107.
35. Dean, J. A., Ed. Lange's Handbook of Chemistry. 14th ed.; McGraw-Hill: New York, 1992; Chapter 8.
36. Edwards, J. O.; Sederstrom, R. J. J. Phys. Chem. 1961, 65, 862.
37. Lide, D. R., Ed. CRC Handbook of Chemistry and Physics, 76th ed.; CRC Press: New York, 1994; pp 8-44.
38. Almarsson, Ö.; Klibanov, A. M. Biotechnol. Bioeng. 1996, 49, 87.
39. Acids and their sodium salts containing bound water were used without dehydration. The small amounts of water introduced by the buffering species should not affect the initial rates since the water activity was independently controlled by salt hydrates (see below).
40. Laitinen, H. A.; Harris, W. E. Chemical Analysis, 2nd ed.; McGrawHill: New York, 1975; p 361.
41. Kuhl, P.; Hailing, P. J.; Jakubke, H.-D. Tetrahetron Lett. 1990, 31, 5213. Kuhl, P.; Hailing, P. J. Biochim. Biophys. Acta 1991, 1078, 326. Kvittingen, L.; Sjursnes, B.; Anthonsen, T.; Hailing, P. J. Tetrahedron 1992, 48, 2793.
42. Kuhl, P.; Hailing, P. J.; Jakubke, H.-D. Tetrahetron Lett. 1990, 31, 5213. Kuhl, P.; Hailing, P. J. Biochim. Biophys. Acta 1991, 1078, 326. Kvittingen, L.; Sjursnes, B.; Anthonsen, T.; Hailing, P. J. Tetrahedron 1992, 48, 2793.
43. Kuhl, P.; Hailing, P. J.; Jakubke, H.-D. Tetrahetron Lett. 1990, 31, 5213. Kuhl, P.; Hailing, P. J. Biochim. Biophys. Acta 1991, 1078, 326. Kvittingen, L.; Sjursnes, B.; Anthonsen, T.; Hailing, P. J. Tetrahedron 1992, 48, 2793.
44. Hailing, P. J. Biotechnol. Tech. 1992, 6, 271. Yang, Z.; Robb, D. A. Biotechnol. Tech. 1993, 7, 37.
45. Hailing, P. J. Biotechnol. Tech. 1992, 6, 271. Yang, Z.; Robb, D. A. Biotechnol. Tech. 1993, 7, 37.
46. 2O the dependence of the enzymatic activity of subtilisin CLCs on the salt concentration (at the 2:3 (mol/mol) ratio of 4 to its conjugate base) leveled off.