Deactivation of Formate Dehydrogenase (FDH) in solution and at gas-liquid interfaces

Biotechnology Progress

Volumn 21, Issue 6, 2005, Pages 1663-1672

  Bommarius, Andreas S ^a,b   Karau, Andreas ^a  

^a EVONIK INDUSTRIES AG   (Germany)

^b GEORGIA INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CONTACTS (FLUID MECHANICS); DRUG PRODUCTS; ESCHERICHIA COLI; SOLUTIONS; STRESSES; VISCOMETERS;

COFACTOR REGENERATION; FORMATE DEHYDROGENASE (FDH); GAS-LIQUID INTERFACES; JONES-DOLE COEFFICIENT;

CATALYST DEACTIVATION;

FORMATE DEHYDROGENASE; INORGANIC SALT; NICOTINAMIDE ADENINE DINUCLEOTIDE; RECOMBINANT PROTEIN;

ARTICLE; BIOREACTOR; BIOTECHNOLOGY; CANDIDA; DRUG ANTAGONISM; ENZYME STABILITY; ENZYMOLOGY; ESCHERICHIA COLI; FLOCCULATION; GAS; GENETIC VARIABILITY; GENETICS; KINETICS; MECHANICAL STRESS; METABOLISM; SOLUTION AND SOLUBILITY; VISCOSITY;

BIOREACTORS; BIOTECHNOLOGY; CANDIDA; ENZYME STABILITY; ESCHERICHIA COLI; FLOCCULATION; FORMATE DEHYDROGENASES; GASES; KINETICS; NAD; RECOMBINANT PROTEINS; SALTS; SOLUTIONS; STRESS, MECHANICAL; VARIATION (GENETICS); VISCOSITY;

CANDIDA BOIDINII; ESCHERICHIA COLI;

EID: 28844501226     PISSN: 87567938     EISSN: None     Source Type: Journal    
DOI: 10.1021/bp050249q     Document Type: Article

References (68)

1. Zaks, A. Industrial biocatalysis. Curr. Opin. Chem. Biol. 2001, 5, 130-136.
2. Liese, A.; Filho, M. V. Production of fine chemicals using biocatalysis. Curr. Opin. Biotechnol. 1999, 10, 595-603.
3. Rozzell, J. D. Biocatalysis at commercial scale: Myths and realities. Chim. Oggi 1999, (6/7), 42-47.
4. for the importance of enantioselectivity to the pharmaceutical industry, see: Crossley, R. Chirality and the Biological Activity of Drugs; CRC Press: Boca Raton, 1995.
5. Bommarius, A. S.; Schwarm, M.; Drauz, K. Factors for process design towards enantiomerically pure L- and D-amino acids. Chimia 2001, 55, 50-59.
6. Zale, S. E.; Klibanov, A. M. Why does ribonuclease irreversibly inactivate at high temperatures? Biochemistry 1986, 25, 5432-5444.
7. Ahern, T. J.; Klibanov, A. M. The mechanisms of irreversible enzyme inactivation at 100°C, Science 1985, 228, 1280-1284.
8. Hickel, A.; Graupner, M.; Lehner, D.; Hermetter, A.; Glatter, O.; Griengl, H. Stability of the hydroxynitrile lyase from Hevea brasiliensis: a fluorescence and dynamic light scattering study. Enzyme Microb. Technol. 1997, 21, 361-366.
9. Rudolph, R.; Haselbeck, A.; Knorr, F.; Jaenicke, R. Reconstruction of rabbit muscle aldolase after dissociation and denaturation at alkaline pH. Hoppe-Seyler's Z. Physiol. Chem. 1978, 359, 867-871.
10. Tirrell, M.; Middleman, S. Shear modification of enzyme kinetics. Biotechnol. Bioeng. 1975, 17, 299-303.
11. Lencki, R. W.; Tecante, A.; Choplin, L. Effect of shear on the inactivation kinetics of the enzyme dextransucrase. Biotechnol. Bioeng. 1993, 42, 1061-1067.
12. Maa, Y.-F.; Hsu, C. C. Effect of high shear on proteins. Biotechnol. Bioeng. 1996, 51, 458-465.
13. Halling, P. J.; Ross, A. C.; Bell, G. Inactivation of enzymes at the aqueous-organic interface. Prog. Biotechnol. 1998, 15, 365-372.
14. Ross, A. C.; Bell, G.; Hailing, P. J. Organic solvent functional group effect on enzyme inactivation by the interfacial mechanism. J. Mol. Catal. B: Enzym. 2000, 8, 183-192.
15. Caussette, M.; Gaunand, A.; Planche, H.; Lindet, B. Enzyme inactivation by inert gas bubbling. Prog. Biotechnol. 1998, 15, 393-398.
16. Caussette, M.; Gaunand, A.; Planche, H.; Monsan, P.; Lindet, B. Inactivation of Enzymes by Inert Gas Bubbling: a kinetic study. Ann. N. Y. Acad. Sci. 1998, 864, 228-233.
17. Caussette, M.; Gaunand, A.; Planche, H.; Colombie, S.; Monsan, P.; Lindet, B. Lysozyme inactivation by inert gas bubbling: kinetics in a bubble column reactor. Enzyme Microb. Technol. 1999, 24, 412-418.
18. Colombie, S.; Gaunand, A.; Lindet, B. Lysozyme inactivation and aggregation in stirred-reactor. J. Mol. Catal. B: Enzym. 2001, 11, 559-565.
19. Quax, W. J.; Mrabet, N. T.; Luiten, R. G. M.; Schuurhuizen, P. W.; Stanssens, P.; Lasters, I. Enhancing the thermostability of glucose isomerase by protein engineering. Biol Technology 1991, 9 (8), 738-742.
20. Kelly, S. T.; Zydney, A. L. Effects of intermolecular thioldisulfide interchange reactions on BSA fouling during microfiltration. Biotechnol. Bioeng. 1994, 44, 972-982.
21. Slusarczyk, H.; Felber, S.; Kula, M. R.; Pohl, M. Stabilization of NAD-dependent formate dehydrogenase from Candida boidinii by site-directed mutagenesis of cysteine residues. Eur. J. Biochem. 2000, 267, 1280-1289.
22. Wichmann, R.; Wandrey, C.; Bückmann, A. F.; Kula, M. R. Continuous enzymatic transformation in an enzyme membrane reactor with simultaneous NADH regeneration. Biotechnol. Bioeng. 1981, 23, 2789-2802.
23. Kula, M.-R.; Wandrey, C. Continuous enzymic transformation in an enzyme-membrane-reactor with simultaneous NADH regeneration. Methods Enzymol. 1987, 136, 9-21.
24. Riebel, B. R. Biochemical and molecular biological characterization of novel microbial NAD(P)-dependent alcohol dehydrogenases. Ph.D. Thesis, University of Düsseldorf, Düsseldorf, Germany, 1997.
25. Hummel, W. New alcohol dehydrogenases for the synthesis of chiral compounds. Adv. Biochem. Eng. 1997, 58, 145-184.
26. Hummel, W.; Schütte, H.; Kula, M.-R. D-2-Hydroxyisocaproate dehydrogenase from Lactobacillus casei. Appl Microbiol. Biotechnol. 1985, 21, 7-15.
27. Schütte, H.; Hummel, W.; Kula, M.-R. L-2-Hydroxyisocaproate dehydrogenase-a new enzyme from Lactobacillus confusus for the stereospecific reduction of 2-ketocarboxylic acids. Appl. Microbiol. Biotechnol. 1984, 19, 167-176.
28. Hummel, W.; Kula, M. R.; Dehydrogenases for the synthesis of chiral compounds. Eur. J. Biochem. 1989, 184, 1-13.
29. Hummel, W. Large-scale applications of NAD(P)-dependent oxidoreductases: recent developments. Trends Biotechnol. 1999, 17, 487-492.
30. Bommarius, A. S. Reduction of C=N-Bonds. In Handbook of Enzyme Catalysis in Organic Synthesis; Drauz, K., Waldmann, H., Eds.; Wiley-VCH: Weinheim, 2002; pp 1047-1063.
31. Bommarius, A. S.; Drauz, K.; Hummel, W.; Kula, M. R.; Wandrey, C. Some new developments in reductive amination with cofactor regeneration. Biocatalysis 1994, 10, 37-48.
32. Bommarius, A. S. Development of enzymatic processes for chiral synthons with emphasis on operational stability. Habilitation thesis, RWTH Aachen, Aachen, Germany, 2000.
33. Ohshima, T.; Soda, K. Biochemistry and biotechnology of amino acid dehydrogenases. Adv. Biochem. Eng. / Biotechnol. 1990, 42, 187-209,
34. Kragl, U.; Vasic-Racki, D.; Wandrey, C. Kontinuierliche Reaktionsführung mit löslichen Enzymen. Chem. Ing. Technol. 1992, 64, 499-509.
35. Hummel, W.; Schütte, H.; Schmidt, E.; Wandrey, C.; Kula, M. R. Isolation of L-phenylalanine dehydrogenase from Rhodococcus sp. M4 and its application for the production of L-phenylalanine. Appl. Microbiol. Biotechnol. 1987, 26, 409-416.
36. Asano, Y.; Yamada, A.; Kato, Y.; Yamaguchi, K.; Hibino, Y.; Hirai, Y.; Kondo, K. Enantioselective synthesis of (S)-amino acids by phenylalanine dehydrogenase from Bacillus sphaericus: Use of natural and recombinant enzymes. J. Org. Chem. 1990, 55, 5567-5571.
37. Bradshaw, C. W.; Wong, C. W.; Hummel, W.; Kula, M. R. Enzyme-catalyzed asymmetric synthesis of (S)-2-amino-4-phenylbutanoic acid and (R)-2-hydroxy-4-phenylbutanoic acid. Biorg. Chem. 1991, 19, 29-39.
38. Hanson, R. L.; Howell, J. M.; LaPorte, T. L.; Donovan, M. J.; Cazzulino, D. L.; Zannella, V. V.; Montana, M. A.; Nanduri, V. B.; Schwarz, S. R.; Eiring, R. F.; Durand, S. C.; Wasylyk, J. M.; Parker, W. L.; Liu, M. S.; Okuniewicz, F. J.; Chen, B.; Harris, J. C.; Natalie, K. J.; Ramig, K.; Swaminathan, S.; Rosso, V. W.; Pack, S. K.; Lotz, B. T.; Bernot, P. J.; Rusowicz, A.; Lust, D. A.; Tse, K. S.; Venit, J. J.; Szarka, L. J.; Patel, R. N. Synthesis of allysine ethylene acetal using phenylalanine dehydrogenase from Thermoactinomyces intermedius. Enzyme Microb. Technol. 2000, 26, 348-358.
39. Bommarius, A. S.; Schwarm, M.; Stingl, K.; Kottenhahn, M.; Huthmacher, K.; Drauz, K. Synthesis and use of enantiomerically pure tert-leucine. Tetrahedron Asymmetry 1995, 6, 2851-2888.
40. Whittaker, M.; Floyd, C. D.; Brown, P.; Gearing, A. J. H. Design and therapeutic application of matrix metalloprotease inhibitors. Chem. Rev. 1999, 99, 2735-2776.
41. Kula, M.-R. Enzyme catalyzed reductions of carbonyl groups. In Chiral Europe; Spring Innovations, Ltd.: Stockport, UK, 1994.
42. Krix, G.; Bommarius, A. S.; Drauz, K.; Kottenhahn, M.; Schwarm, M.; Kula, M. R. Enzymatic reduction of α-keto acids leading to L-amino acids or D-hydroxy Acids. J. Biotechnol. 1997, 53, 29-39.
43. Slusarczyk, H. Stabilization of NAD-dependent formate dehydrogenase from Candida boidinii by site-directed mutagenesis. Ph.D. Thesis, Heinrich-Heine University Düsseldorf, Düsseldorf, Germany, 1997.
44. Lamzin, V. S.; Aleshin, A. E.; Strokopytov, B. V.; Yukhnevich, M. G.; Popov, V. O.; Harutyunyan, E. H.; Wilson, K. S. Crystal structure of NAD-dependent formate dehydrogenase. Eur. J. Biochem. 1992, 206, 441-52.
45. Hofmeister, F. Zur Lehre von der Wirkung der Salze. Zweite Mitteilung. Arch. Exp. Pathol. Pharmakol. 1888, 24, 247-260.
46. Setschenow, J. Über die Konstitution der Salzlösungen auf Grund ihres Verhaltens zu Kohlensäure. Z. Physik. Chem. 1889, 4, 117-125.
47. von Hippel, P. H.; Wong, K.-Y. Neutral salts: the generality of their effects on the stability of macromolecular conformation. Science 1904, 145, 577-580.
48. Sinanoglu, O.; Abdulnur, S. Effect of water and other solvents on the structure of biopolymers. Fed. Proc. 1965, 24, S12-S23.
49. Grigorjew, P. A.; Bezrukov, S. M. Hofmeister effect in ion transport - reversible binding of halide anions to the roflamycoin channel. Biophys. J. 1994, 67, 2265-2271.
50. Kirkwood, J. G. In Proteins, Amino Acids and Peptides; Cohn, E. J., Edsall, E. T., Eds.; Reinhold: New York, 1943; pp 276-303.
51. Melander, W.; Horvath, C. Salt effects on hydrophobic interactions in precipitation and chromatography of proteins: An interpretation of the lyotropic series. Arch. Biochem. Biophys. 1977, 183, 200-215.
52. Cohn, E. J.; Edsall, E. T. Proteins, Amino Acids and Peptides; Reinhold: New York, 1943.
53. Washabaugh, M. W.; Collins, K. D. The Hofmeister effect and the behaviour of water at interfaces. Q. Rev. Biophys. 1985, 18, 323-422;
54. Collins, K. D. Sticky ions in biological systems. Proc. Natl. Acad. Sci. U.S.A. 1995, 92, 5553-5557.
55. Collins, K. D. Charge density-dependent strength of hydration and biological structure. Biophys. J. 1997, 72, 65-76.
56. Kiriukhin, M. Y.; Collins, K. D. Dynamic hydration numbers for biologically important ions. Biophys. Chem. 2002, 99, 155-168.
57. Collins, K. D. Ions from the Hofmeister series and osmolytes: effects on proteins in solution and in the crystallization process. Methods 2004, 34, 300-311.
58. Jones, G.; Dole, M. The viscosity of aqueous solutions of strong electrolytes with special reference to barium chloride. J. Am. Chem. Soc. 1929, 51, 2950-2964.
59. Podobolsky, R. J. Transport process in electrolyte solutions. J. Phys. Chem. 1958, 80, 4442-4451.
60. Bradford, M. M. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. J. Anal. Biochem. 1976, 72, 248-254.
61. von Smoluchowski, M. Versuch einer mathematischen Theorie der Koagulationskinetik kolloidaler Lösungen. Z. Physik. Chem. 1917, 92, 129-168.
62. Wandrey, C. Reaction Engineering Investigations on Enzyme Catalysts for the Development of Continuous Processes. Habilitation thesis, TH Hannover, Hannover, Germany, 1977.
63. Bommarius, A. S.; Riebel, B. R. Biocatalysis - Fundamentals and Applications; Wiley-VCH: New York, 2004; Chapters 2 and 5.
64. Hine, J. Physical Organic Chemistry, 2nd ed.; McGraw-Hill: New York, 1962; pp 73-75.
65. Middleman, S. Introduction to Heat and Mass Transfer, 3rd ed.; Wiley-Interscience: New York, 1999; Chapter 7.
66. Lee, S.-H.; Ruckenstein, E. Adsorption of proteins onto polymeric surfaces of different hydrophilicities - a case study with bovine serum albumin. J. Colloid Interface Sci. 1988, 125, 365-379.
67. Breslow, R.; Guo, T. Surface tension measurements show that chaotropic salting-in denaturants are not just water-structure breakers. Proc. Natl. Acad. Sci. U.S.A. 1990, 87, 167-169.
68. Lin, T.-Y.; Timasheff, S. N. On the role of surface tension in the stabilization of globular proteins. Protein Sci. 1996, 5, 372-381.