Investigating pH and Cu (II) effects on lipase activity and enantioselectivity via kinetic and spectroscopic methods

Biotechnology Journal

Volumn 1, Issue 11, 2006, Pages 1293-1301

  Xu, Tian Wen ^a   Xu, Jian He ^a   Yu, Wei ^b   Zhong, Ju Hua ^c  

^a EAST CHINA UNIVERSITY OF SCIENCE AND TECHNOLOGY   (China)

^b BEIJING UNIVERSITY OF POSTS AND TELECOMMUNICATIONS   (China)

^c EAST CHINA UNIVERSITY OF SCIENCE AND TECHNOLOGY   (China)

Author keywords

1 Phenethyl acetate; Candida rugosa lipase; Conformation modulation; Enantioselectivity; Hydrolytic activity

Indexed keywords

1-PHENETHYL ACETATE; ACIDIC PH; ACTIVATION FREE ENERGY; CANDIDA RUGOSA LIPASE; CATALYTIC MECHANISMS; CONFORMATIONAL CHANGE; COPPER IONS; DIFFERENT EFFECTS; FLUORESCENCE EMISSION SPECTRA; HYDROLYTIC ACTIVITIES; KINETIC BEHAVIOR; LIPASE ACTIVITY; MICROENVIRONMENTS; NEUTRAL PH; PROTEIN CONFORMATION; REACTION MEDIUM; SPECTROSCOPIC METHOD; SPECTROSCOPIC TECHNIQUE; STRUCTURAL BASIS; UV-VISIBLE;

CANDIDA; COPPER; EMISSION SPECTROSCOPY; ENZYME ACTIVITY; PH EFFECTS; SPECTROSCOPIC ANALYSIS; VOLATILE FATTY ACIDS;

ENANTIOSELECTIVITY;

ACETIC ACID DERIVATIVE; COPPER; TRIACYLGLYCEROL LIPASE;

ARTICLE; CANDIDA; CHEMICAL MODEL; CHEMISTRY; ENZYMOLOGY; HYDROLYSIS; KINETICS; METABOLISM; METHODOLOGY; PH; POLYACRYLAMIDE GEL ELECTROPHORESIS; RAMAN SPECTROMETRY; SPECTROFLUOROMETRY; SPECTROPHOTOMETRY; STEREOISOMERISM; THERMODYNAMICS; ULTRAVIOLET RADIATION;

ACETATES; CANDIDA; COPPER; ELECTROPHORESIS, POLYACRYLAMIDE GEL; HYDROGEN-ION CONCENTRATION; HYDROLYSIS; KINETICS; LIPASE; MODELS, CHEMICAL; SPECTROMETRY, FLUORESCENCE; SPECTROPHOTOMETRY; SPECTRUM ANALYSIS, RAMAN; STEREOISOMERISM; THERMODYNAMICS; ULTRAVIOLET RAYS;

EID: 39049181354     PISSN: 18606768     EISSN: 18607314     Source Type: Journal    
DOI: 10.1002/biot.200600135     Document Type: Article

References (44)

1. Salilas, B., Ashok, P., Candida rugosa lipases: Molecular biology and versatility in biotechnology. Yeast 1998, 14, 1069-1087.
2. Palomo, J. M., Fernandez-Lorente, G., Mateo, C., Fuentes, M. et al., Modulation of the enantioselelctivity of Candida antarctica B lipase via conformational engineering: kinetic resolution of (±)-α-hydroxyphenylacetic acid derivatives. Tetrahedron: Asymmetry 2002, 13, 1337-1345.
3. Cygler, M., Schrag, J. D., Structure and conformational flexibility of Candida rugosa lipase. Biochim. Biophys. Acta 1999, 1441, 205-214.
4. Battinelli, L., Cernia, E., Delbò, M., Ortaggi, G. et al., New class of poly(vinyl alcohol) polymers as column-chromatography stationary phases for Candida rugosa lipase isoforms separation. J. Chromatography 1996, 753, 47-55.
5. Belleza, F., Cipiciani, A., Costanti, U., Esterase activity of biocomposites constituted by lipases adsorbed on layered zirconium phosphate and phosphonates: selective adsorption of different enzyme isoforms. J. Mol. Catal. B: Enzym. 2003, 26, 47-56.
6. Rua, L., Diaz-Maurino, T., Fernandez, V. M., Otero, C. et al., Purification and characterization of two distinct lipases from Candida cylindracea. Biochim. Biophys. Acta 1993, 1156, 181-189.
7. Sabuquillo, P., Reina, J., Fernandez-Lorente, G., Guisan, J. M. et al., 'Interfacial affinity chromatography' of lipases: separation of different fractions by selective adsorption on supports activated with hydrophobic groups. Biochim. Biophys. Acta 1998, 1388, 337-348.
8. Grochulski, P., Li, Y., Schrag, J. D., Bouthillier, F. et al., Insights into interfacial activation from an open structure of Candida rugosa lipase. J. Biol. Chem. 1993, 268, 12843-12847.
9. Mancheño, J. M., Pernas, M. A., Martínez, M. J., Ochoa, B. et al., Structural insights into the lipase/esterase behavior in the Candida rugosa lipases family: crystal structure of the lipase 2 isoenzyme at 1.97A resolution. J. Mol. Biol. 2003, 332, 1059-1069.
10. Grochulski, P., Li, Y., Schrag, J. D., Cygler M., Two conformational states of Candida rugosa lipase. Protein Sci. 1992, 3, 82-91.
11. James, J. J., Lakshmi, B. S., Raviprasad, V., Ananth, M. J. et al., Insights from molecular dynamics simulations into pH-dependent enantioselectivity hydrolysis of ibuprofen esters by Candida rugosa lipase. Protein Eng. 2003, 16, 1017-1024.
12. Liu, Y. Y., Xu, J. H., Xu, Q. G., Hu, Y., Significant enhancement of lipase enantioselectivity towards (S)-ketoprofen ester at pH 2. Biotechnol. Lett. 1999, 21, 143-146.
13. Wu, S. H., Guo, W., Sih, C. J., Enhancing the enantioselectivity of Candida lipase-catalyzed ester hydrolysis via noncovalent enzyme modification. J. Am. Chem. Soc. 1990, 112, 1990-1995.
14. Holmberg, E., Hulk, K., Temperature as enantioselective parameters in enzymatic resolutions of racemic mixtues. Biotechnol. Lett. 1991, 13, 323.
15. Kahlow, U. H. M., Schmid, R. D., Pleiss, J., A model of the pressure dependence of the enantioselectivity of Candida rugosa lipase towards (±)-menthol. Protein Sci. 2001, 10, 1942-1952.
16. Liu, Y. Y., Xu, J. H., Hu, Y., Enhancing effect of Tween-80 on lipase performance in enantioselectivity hydrolysis of ketoprofen ester. J. Mol. Catal. B: Enzym. 2000, 10, 523-529.
17. Okamoto, T., Ueji, S., A new method for improving the enantioselectivity of lipase-catalyzed hydrolysis in organic solvent containing a small amount of water in the presence of metal ions. Biotechnol. Lett. 2000, 22, 1169-1171.
18. Watanabe, K., Ueji, S., Dimethyl sulfoxide as a co-solvent dramatically enhances the enantioselectivity in lipase-catalysed resolutions of 2-phenoxy-propionic acyl derivatives. J. Chem. Soc., Perkin Trans. 2001, 1, 1386-1390.
19. Herniz, M. J., Snchez-Montero, J. M., Sinisterra, J. V., Influence of the nature of modifier in the enzymatic activity of chemical modified semipurified lipase from Candida rugosa. Biotechnol. Bioeng. 1997, 55, 252-260.
20. Wescott, C. R., Klibanov, A. M., The solvent dependence of enzyme specificity. Biochim. Biophys. Acta 1994, 1206, 1-9.
21. Pelton, J. T., Mclean, L. R., Spectroscopic methods for analysis of protein secondary structure. Anal. Biochem. 2000, 227, 167-176.
22. Otero, C., Rúa, M. L., Robledo, L., Influence of the hydrophobicity of lipase isoenzymes from Candida rugosa on its hydrolytic activity in reverse micelles. FEBS Lett. 1995, 360, 202-206.
23. Cernia, E., Delfini, M., Di Cocco, E., Palocci C. et al., Investigation of lipase-catalysed hydrolysis of naproxen methyl ester: use of NMR spectroscopy methods to study substrate-enzyme interaction. Bioorg. Chem. 2002, 30, 276-284.
24. Monecke, P., Friedemann, R., Naumann, S., Csuk, R., Molecular modeling studies on the mechanism of Candida rugosa lipase. J. Mol. Model. 1998, 4, 395-404.
25. Egri, G., Kolbert, A., Blint, J., Fogassy, E. et al., Baker's yeast mediated stereoselective biotransformation of 1-acetoxy-3-aryloxypropan-2-ones. Tetrahedron: Asymmetry 1998, 9, 271-283.
26. Liu, Y. Y., Xu, J. H., Wu, H. Y., Shen, D., Integration of purification with immobilization of Candida rugosa lipase for kinetic resolution of racemic ketoprofen. J. Biotechnol. 2004, 110, 209-217.
27. Chen, C. S., Fujimoto, Y., Girdaukas, G., Sih, C. J., Quantitative analyses of biochemical kinetic resolution of enantiomers. J. Am. Chem. Soc. 1982, 104, 7294-7299.
28. Robert, A. C., Enzymes: A practical introduction to structure, mechanism, and data analysis (second edition). Wiley-VCH, New York 2000, pp. 109-145.
29. Bradford, M. M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of proteindye binding. Anal. Biochem. 1976, 72, 248-254.
30. Ottosson, J., Hult, K., Influence of acyl chain length on the enantioselectivity of Candida antarctica lipase B and its thermodynamic components in kinetic resolution of sec-alcohols. J. Mol. Catal. B: Enzym. 2001, 11, 1025-1028.
31. Ottosson, J., Rotticci-Mulder, Rotticci, J. C., Hult, K., Rational design of enantioselective enzymes requires considerations of entropy. Protein Sci. 2001, 10, 1769-1774.
32. Ottosson, J., Fransson, L., King, J. W., Hult, K., Size as a parameter for solvent effects on Candida antarctica lipase B enantioselectivity. Biochim. Biophys. Acta 2002, 1594, 325-334.
33. Phillips, R. S., Temperature modulation of the stereochemistry of enzymatic catalysis: prospects for exploitation. Trends Biotechnol. 1996, 14, 13-16.
34. Lozano, P., de Diego, T., Iborra, J. L., Dynamic structure/function relationship in the 〈 -chymotrypsin deactivation process by heat and pH. Eur. J. Biochem. 1997, 248, 80-85.
35. Brady, L., Brzozowski, A. M., Derewenda, Z. S., Dodson, E. et al., A serine protease triad forms the catalytic centre of a triacylglycerol lipase. Nature 1990, 343, 767-770
36. del-Val, M. I., Otero, C., Kinetic and spectroscopic behaviour of a lipase-microgel derivative in aqueous and micellar media. J. Mol. Catal. B: Enzym. 1998, 4, 137-147.
37. Liu, B. K. S., Tyryshkin, A. M., Roberts, A. G., Bowman, M. K. et al., Inhibitory copper binding site on the spinach cytochrome b(6)f complex: Implication for Q(0) site catalysis. Biochemistry 2000, 39, 3285-3296.
38. Viles, J. H., Cohen, F. E., Prusiner, S. B., Goodin, D. B. et al., Copper binding to the prion protein: Structural implication of four identical cooperative binding sites. Proc. Natl. Acad. Sci. USA 1999, 96, 2042-2047.
39. Miura, T., Suzuki, K., Kohata, N., Takeuchi, H., Metal coordination modes of Alzheimer's amyloid β-peptide in insoluble aggregates and soluble complexes. Biochemistry 2000, 39, 7024-7031.
40. Pattabhi, V., Gautham, N., Biophysics. Delhi Kluwer Academic Publishers, Boston 2002, pp. 59-74.
41. Lawrence, Q. J., Physical methods in bioinorganic chemistry: spectroscopy and magnetism. University Science Books, California 2000, pp. 21-27.
42. Kubelka, J., Pancoska, P., Keiderling, T. A., Novel use of a static modification of two-dimensional correlation analysis. Part II: Hetro-spectral correlations of protein Raman, FT-IR, and circular dichroism spectra. Appl. Spectrosc. 1999, 53, 666-671.
43. Yeo, S. D., Debenedetti, P. G., Patro, S. Y., Przybycien, T. M., Secondary structure characterization of microparticulate insulin powders. J. Pharm. Sci. 1994, 83, 1651-1656
44. Susi, H., Byler, D. M., Fourier deconvolution of the Amide I Raman band of proteins as related to conformation. Appl. Spectrosc. 1998, 42, 819-826