Time-dependent structure and activity changes of α-chymotrypsin in water/alcohol mixed solvents

Bioscience, Biotechnology and Biochemistry

Volumn 64, Issue 12, 2000, Pages 2552-2558

  Sato, Makiko ^a   Sasaki, Toshiya ^a   Kobayashi, Masami ^a   Kise, Hideo ^a  

^a UNIVERSITY OF TSUKUBA   (Japan)

Author keywords

Circular dichroic (CD) spectroscopy; Time dependent structure change; Transesterification; Water alcohol mixed solvent; Chymotrypsin

Indexed keywords

ALCOHOL; ALCOHOL DERIVATIVE; CHYMOTRYPSIN; CHYMOTRYPSIN A; METHANOL; SOLVENT; TRIFLUOROETHANOL; WATER;

ARTICLE; CHEMISTRY; CIRCULAR DICHROISM; KINETICS; METABOLISM; PROTEIN CONFORMATION; STRUCTURE ACTIVITY RELATION; TIME;

ALCOHOLS; CHYMOTRYPSIN; CIRCULAR DICHROISM; ETHANOL; KINETICS; METHANOL; PROTEIN CONFORMATION; SOLVENTS; STRUCTURE-ACTIVITY RELATIONSHIP; TIME FACTORS; TRIFLUOROETHANOL; WATER;

EID: 0034573685     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.64.2552     Document Type: Article

References (19)

1. Wong, C. H. and Whitesides, G. M., Use of hydrolytic enzymes: amidases, proteases, esterases, lipases, nitrilases, phosphatases, epoxide hydrolases. In:Enzymes in Synthetic Organic Chemistry.Elsevier Science Ltd., Oxford, U.K., pp. 41-130 (1994).
2. Halling, P. J., Thermodynamic predictions for biocatalysis in nonconventional media: Theory, tests, and recommendations for experimental design and analysis.Enzyme Microb. TechnoL,16, 178-206 (1994).
3. Gill, I., Lopez-Fandino, R., Jorba, X., and Vulfson, E. N., Biologically active peptides and enzymatic approaches to their production.Enzyme Microb. Technol., 18, 162-183 (1996).
4. Kise, H., Fujimoto, K., and Noritomi, H., Enzymatic reactions in aqueous-organic media. VI. Peptide synthesis by a-chymotrypsin in hydrophilic organic solvents.J. Biotechnol.,8, 279-290 (1988).
5. Ru, M. T., Dordick, J. S., Reimer, J. A., and Clark, D. S., Optimizing the salt-induced activation of enzymes in organic solvents: effects of lyophilization time and water content.Biotechnol. Bioeng.,63, 233-241 (1999).
6. Tomiuchi, Y., Kijima, T., and Kise, H., Fluorescence spectroscopic study of a-chymotrypsin as relevant to catalytic activity in aqueous-organic media.Bull. Chem. Soc. Jpn.,66, 1176-1181 (1993).
7. Kijima, T., Yamamoto, S., and Kise, H., Study on tryptophan fluorescence and catalytic activity ofα-chymotrypsin in aqueous-organic media.Enzyme Microb. Technol.,18, 2-6 (1996).
8. Manavalan, P. and Johnson, Jr., W. C., Sensitivity of CD to protein tertiary structure class.Nature,305, 831-832 (1983).
9. Wu, J., Yang, J. T., and Wu, C.-S. C., β-II conformation of all-β proteins can be distinguished from unordered form by CD.Anal. Biochem.,200, 359-364 (1992).
10. Morrisett, J. D. and Broomfield, C. A., Active site spin-labeled a-chymotrypsin. Guanidine hydrochloride denaturation studies using EPR and CD.J. Am. Chem. Soc.,93, 7297-7304 (1971).
11. Hennessey Jr., J. P., and Johnson Jr., W. C., Information content in CD of proteins.Biochemistry,20, 1085-1094 (1981).
12. Sasaki, T., Kobayashi, M., and Kise, H., Active conformation of a-chymotrypsin in organic solvents as studied by circular dichroism.Biotechnol. Lett.,11, 387-390 (1997).
13. Teale, F. W. J., The ultraviolet fluorescence of proteins in neutral solutions.Biochem. J.,76, 381-388 (1960).
14. Gabel, D., Steinberg, I. Z., and Katchalski, E., Changes in conformation of insolubilized trypsin and chymotrypsin, followed by fluorescence.Biochemistry,10, 4661-4669 (1971).
15. Benson, D. R., Hart, B. R., Zhu, X., and Doughty, M. B., Design, synthesis and CD investigation of a peptide-sandwiched mesoheme, J. Am. Chem. Soc.,117, 8502-8510 (1995).
16. De Laureto, P. P., De Filippis, V., Scaramella, E., Zambonin, M., and Fontana, A., Limited proteolysis of lysozyme in trifluoroethanol. Isolation and characterization of a partially active enzyme derivative.Eur. J. Biochem.,230, 779-787 (1995).
17. Arunkumar, A. I., Kumar, T. K. S., Jayaraman, G., Samuel, D., and Yu, C., Induction of helical conformation in all β-sheet proteins by trifluoroethanol.J. Biomol. Struc. Dynamics,14, 381-385 (1996).
18. Dong, A., Matsuura, J., Manning, M. C., and Carpenter, J. F., Intermolecular β-sheet results from trifluoroethanol-induced nonnative ce-helical structure in β-sheet predominant proteins: infrared and circular dichroism spectroscopic study.Arch. Biochem. Biophys.,355, 275-281 (1998).
19. Dong, A., Meyer, J. D., Kendrick, B. S., Manning, M. C., and Carpenter, J. F., Effect of secondary structure on the activity of enzymes suspended in organic solvents.Arch. Biochem. Biophys.,334, 406-414 (1996).