Effects of methanol on the catalytic properties of porcine pancreatic lipase

Journal of Microbiology and Biotechnology

Volumn 15, Issue 2, 2005, Pages 296-301

  Park, Hyun ^a   Lee, Ki Seog ^c   Chi, Young Min ^c   Jeong, Seung Weon ^b  

^a Korea Polar Research Institute (KOPRI)   (South Korea)

^b Korea Food Research Institute   (South Korea)

^c Korea University   (South Korea)

Author keywords

Hydrolysis; Lipase; Methanol solvent; Methanolysis; Rate limiting step

Indexed keywords

METHANOL; TRIACYLGLYCEROL LIPASE;

ARTICLE; BINDING COMPETITION; CATALYSIS; CHEMICAL STRUCTURE; DEACYLATION; ENZYME ACTIVITY; ENZYME ANALYSIS; FLUORESCENCE ANALYSIS; HYDROPHOBICITY; NONHUMAN; SWINE;

SUIDAE;

EID: 18144424850     PISSN: 10177825     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (22)

1. Affleck, R., C. A. Haynes, and D. S. Clark. 1992. Solvent dielectric effects on protein dynamics. Proc. Natl. Acad. Sci. USA 89: 5167-5170.
2. Brady, L., A. M. Brzozowski, Z. S. Derewenda, E. Dodson, G. Dodson, S. Tolley, J. P. Turkenburg, L. Christiansen, B. Huge-Jensen, L. Norskov, L. Thim, and U. Menge. 1990. A serine protease triad forms the catalytic centre of a tryacylglycerol lipase. Nature 343: 767-770.
3. Burdette, R. A. and D. M. Quinn. 1986. Interfacial reaction dynamics and acylenzyme mechanism for lipoprotein lipase-catalyzed hydrolysis of lipid p-nitrophenyl ester. J. Biol. Chem. 261: 12016-12021.
4. Cartwright, S. J. and S. G. Waley. 1987. Cryoenzymology of β lactamases. Biochemistry 26: 5329-5337.
5. Compton, P. D., R. J. Coll, and A. L. Fink. 1986. Effect of methanol cryosolvents on the structural and catalytic properties of bovine trypsin. J. Biol. Chem. 261: 1248-1252.
6. α-benzyloxycarbonyl-L-lysine-p-nitrophenyl ester in dimethylsulfoxide at subzero temperature. J. Biol. Chem. 249: 5027-5032.
7. Hilton, S. and J. T. Buckley. 1991. Studies on the reaction mechanism of a microbial lipase/acyltransferase using chemical modification and site-directed mutagenesis. J. Biol. Chem. 266: 997-1000.
8. Kazlauskas, R. J. 1994. Elucidating structure-mechanism relationships in lipases: Prospects for predicting and engineering catalytic properties. Trends Biotechnol. 12: 464-472.
9. Lemke, K., M. Lemke, and F. Theil. 1997. A three-dimensional predictive active site model for lipase from Pseudomonas cepacia. J. Org. Chem. 63: 6268-6273.
10. Moreau, H., A. Moulin, Y. Gargouri, J. Noël, and R. Verger. 1991. Inactivation of gastric and pancreatic lipases by diethyl p-nitrophenyl phosphate. Biochemistry 30: 1037-1041.
11. Paiva, A. L., V. M. Balcão, and F. X. Malcata. 2000. Kinetics and mechanisms of reactions catalyzed by immobilized lipases. Enzyme Microb. Technol. 27: 187-204.
12. Park, H. and Y. M. Chi. 2001. The enhancement of electrostriction caused by lowering the solvent dielectric constant leads to the decrease of activation energy in trypsin catalysis. Biochim. Biophys. Acta 1568: 53-59.
13. Peters, G. H., D. M. F. van Aalten, O. Edholm, S. Toxvaerd, and R. Bywater. 1996. Dynamics of proteins in different solvent systems: Analysis of essential motion in lipases. Biophys. J. 71: 2245-2255.
14. Peters, G. H., S. Toxvaerd, O. H. Olsen, and A. Svendsen. 1997. Computational studies of the activation of lipase and the effect of a hydrophobic environment. Protein Eng. 10: 137-147.
15. Petersen, M. T. N., P. Fojan, and S. B. Petersen. 2001. How do lipases and esterases work: The electrostatic contribution. J. Biotechnol. 85: 115-147.
16. Reyes, H. R. and C. G. Hill. 1993. Kinetic modeling of interesterification reactions catalyzed by immobilized lipase. Biotechnol. Bioengin. 43: 171-182.
17. Stevanato, R., B. Mondovi, O. Befani, M. Scarpa, and A. Rigo. 1994. Electrostatic control of oxidative deamination catalyzed by bovine serum amine oxidase. Biochem. J. 299: 317-320.
18. Stryer, L. 1995. Biochemistry, 4th Ed. pp. 207-210. W. H. Freeman & Company, NY, U.S.A.
19. Svendsen, A. 2000. Lipase protein engineering. Biochim. Biophys. Acta 1543: 223-238.
20. Villeneuve, P., J. M. Muderhwa, J. Graille, and M. J. Haas. 2000. Customizing lipases for biocatalysis: A survey of chemical, physical and molecular biological approaches. J. Mol. Catal. B: Enzymatic 9: 113-148.
21. Warshel, A., G. Naray-Szabo, F. Sussman, and J. K. Hwang. 1989. How do serine proteases work? Biochemistry 28: 3629-3637.
22. Zandonella, G., P. Stadler, L. Haalck, F. Spener, F. Paltauf, and A. Hermetter. 1999. Interactions of fluorescent triacylglycerol analogs covalently bound to the active site of a lipase from Rhizopus oryzae. Eur. J. Biochem. 262: 63-69.