Effect of lipase-lipase interactions in the activity, stability and specificity of a lipase from Alcaligenes sp.

Enzyme and Microbial Technology

Volumn 39, Issue 2, 2006, Pages 259-264

  Wilson, Lorena ^b   Palomo, José M ^a   Fernández Lorente, Gloria ^a   Illanes, Andrés ^b   Guisán, José M ^a   Fernández Lafuente, Roberto ^a  

^a CSIC   (Spain)

^b PONTIFICIA UNIVERSIDAD CATÓLICA DE VALPARAÍSO   (Chile)

Author keywords

Interfacial activation; Lipase QL from Alcaligenes sp.; Lipase lipase interaction; Protein immobilization

Indexed keywords

BIOCATALYSTS; DETERGENTS; DIMERS; ENZYMES; GENES; MONOMERS;

INTERFACIAL ACTIVATION; LIPASE QL FROM ALCALIGENES SP.; LIPASE-LIPASE INTERACTION; PROTEIN IMMOBILIZATION;

PROTEINS;

DETERGENT; DIMER; MONOMER; TRIACYLGLYCEROL LIPASE; TRITON X 100;

ALCALIGENES; ARTICLE; BIOCATALYST; ENANTIOSELECTIVITY; ENZYME ACTIVITY; ENZYME IMMOBILIZATION; ENZYME ISOLATION; ENZYME SPECIFICITY; ENZYME STABILITY; GEL FILTRATION; PROTEIN PROTEIN INTERACTION; SUPERNATANT; THERMOSTABILITY;

ALCALIGENES; ALCALIGENES SP.;

EID: 33646535438     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2005.10.015     Document Type: Article

References (35)

1. Wong C.-H., and Whitesides G.M. In: Baldwin J.E., and Magnus F.R.S. (Eds). Enzymes in synthetic organic chemistry. Tetrahedron organic chemistry series vol. 12 (1994), Pergamon 41-130
2. Virto C., Svensson I., and Adlercreutz P. Enzymatic synthesis of lysophosphatidic acid and phosphatidic acid. Enzyme Microb Technol 24 (1999) 651-658
3. Weissfloch A.N.E., Kazlauskas R.J., and Marchessault R.H. Enantiopreference of Lipase from Pseudomonas cepacia toward primary alcohols. J Org Chem 60 (1995) 6959-6969
4. Sarda L., and Desnuelle P. Action de la lipase pancréatique sur les esteres en emulsion. Biochim Biophys Acta 30 (1958) 513-521
5. Brady L., Brzozowski A.M., Derewenda Z.S., Dodson E., Dodson G., Tolley S., et al. A serine protease triad forms the catalytic center of a triacylflycerol lipase. Nature 343 (1990) 767-770
6. Winkler F.K., D'Arcy A., and Hunziker W. Structure of human pancreatic lipase. Nature 351 (1990) 771-774
7. Brzozowski A.M., Derewenda Z.S., Dodson G.G., Lawson D.M., Turkenberg J.P., Bjorkling F., et al. A model for interfacial activation in lipases from the structure of a fungal lipase-inhibitor complex. Nature 351 (1991) 491-494
8. Nobel M.E.M., Cleasby A., Johnson L.N., Egmond M.R., and Frenken L.G.J. The crystal structure of triacylglycerol lipase from Pseudomonas glumae reveals a partial redundant catalytic aspartate. FEBS Lett 331 (1993) 1265-1269
9. Derewenda Z.S., and Derewenda U. The crystal and molecular structure of the Rhizomucor miehei triacylglyceride lipase at 1.9 Å resolution. J Mol Biol 227 (1992) 818-839
10. Ampon K., Basri M., Salleh A.B., Wan Yunus W.M.Z., and Razak C.N.A. Immobilization by adsorption of hydrophobic lipase derivatives to porous polymer beads for use in ester synthesis. Biocatalysis 10 (1994) 341-351
11. Kerzel P., and Mersmann A. Adsorption behaviour of lipase from Staphylococcus carnosa on a hydrophobic adsorbent. J Chromatogr 584 (1992) 109-113
12. Norin M., Boutleje J., Holmberg E., and Hult K. Lipase immobilized by adsorption. Effect of the support hydrophobicity on the reaction rate of ester synthesis in cyclohexane. Appl Microb Technol 28 (1988) 527-530
13. Bastida A., Sabuquillo P., Armisén P., Fernández-Lafuente R., Huguet J., and Guisán J.M. A single step purification, immobilization and hyperactivation of lipases via interfacial adsorption on strongly hydro-phobic supports. Biotechnol Bioeng 58 (1998) 486-493
14. Fernández-Lafuente R., Armisén P., Sabuquillo P., Fernández-Lorente G., and Guisán J.M. Immobilization of lipases by selective adsorption on hydrophobic supports. Chem Phys Lipids 93 (1998) 185-197
15. Sugiura M., and Isobe M. Studies on the mechanism of the lipase reaction. I. Inhibition of lipase activity by emulsion of organic solvents. Chem Pharm Bull 23 (1975) 1221-1225
16. Sugiura M., and Isobe M. Studies on the mechanism of lipase reaction. III. Adsorption of Chromobacterium lipase on hydrophobic glass beads. Chem Pharm Bull 24 (1976) 72-78
17. Sugiura M., and Isobe M. Studies on the mechanism of lipase reaction. IV. Action of the lipase from Chromobacterium on monomeric p-nitrophenyl acetate. Chem Pharm Bull 24 (1976) 1822-1828
18. Sugiura M., and Isobe M. Purification of microbial lipases by glass beads coated with hydrophobic materials. Chem Pharm Bull 23 (1977) 1221-1225
19. Fernández-Lorente G., Palomo J.M., Fuentes M., Mateo C., Guisán J.M., and Fernández-Lafuente R. Self-assembly of Pseudomonas fluorescens lipase into bimolecular aggregates dramatically affects functional properties. Biotechnol Bioeng 82 (2003) 232-237
20. Palomo J.M., Fuentes M., Fernández-Lorente G., Mateo C., Guisán J.M., and Fernández-Lafuente R. General trend of lipase to self-assemble giving bimolecular aggregates greatly modifies the enzyme functionality. Biomacromolecules 4 (2003) 1-6
21. Palomo J.M., Ortiz C., Fuentes M., Fernández-Lorente G., Guisán J.M., and Fernández-Lafuente R. Use of immobilized lipases for lipase purification via specific lipase-lipase interactions. J Chromatogr A 1038 (2004) 267-273
22. Palomo J.M., Ortiz C., Fernández-Lorente G., Fuentes M., Guisán J.M., and Fernández-Lafuente R. Lipase-lipase interactions as a new tool to immobilize and modulate the lipase properties. Enzyme Microb Technol 36 (2005) 447-454
23. Muralidhar R.V., Chirumamilla R.R., Marchant R., Ramachandran V.N., Ward O.P., and Nigam P. Understanding lipase stereoselectivity. World J Microbiol Biotechnol 18 (2002) 81-97
24. Naemura K., Murata M., Tanaka R., Yano M., Hirose K., and Tobe Y. Enantioselective acylation of alcohols catalyzed by lipase QL from Alcaligenes sp.: a predictive active site model for lipase QL to identify the faster reacting enantiomer of an alcohol in this acylation. Tetrahedron: Asymmetry 7 (1996) 1581-1584
25. Naemura K., Murata M., Tanaka R., Yano M., Hirose K., and Tobe Y. Enantioselective acylation of primary and secondary alcohols catalyzed by lipase QL from Alcaligenes sp.: a predictive active site model for lipase QL to identify which enantiomer of an alcohol reacts faster in this acylation. Tetrahedron: Asymmetry 7 (1996) 3285-3294
26. Tanaka K., and Yasuda M. A practical synthesis of (R)-3-chlorostyrene oxide starting from 3-chloroethylbenzene. Tetrahedron: Asymmetry 9 (1998) 3275-3282
27. Sharfuddin M., Narumi A., Iwai Y., Miyazawa K., Yamada S., Kakuchi T., et al. Lipase-catalyzed dynamic kinetic resolution of hemiaminals. Tetrahedron: Asymmetry 14 (2003) 1581-1585
28. Negishi S., Shirasawa S., Arai Y., Suzuki J., and Mukataka S. Activation of powdered lipase by cluster water and the use of lipase powders for commercial esterification of food oils. Enzyme Microb Technol 32 (2003) 66-70
29. Palomo J.M., Segura R., Mateo C., Fernández-Lafuente R., and Guisán J.M. Improving the activity of lipases from thermophilic organisms at mesophilic temperatures for biotechnology applications. Biomacromolecules 1 (2004) 249-254
30. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 277 (1970) 680-685
31. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72 (1976) 248-254
32. Palomo J.M., Muñoz G., Fernández-Lorente G., Mateo C., Fernández-Lafuente R., and Guisán J.M. Interfacial adsorption of lipases on very hydrophobic support (Octadecyl Sepabeads): immobilization, hyperactivation and stabilization of the open form of lipases. J Mol Catal B: Enzym 19-20 (2002) 279-286
33. Segura R., Palomo J.M., Mateo C., Cortés A., Terreni M., Fernández-Lafuente R., et al. Different properties of the lipases contained in porcine pancreatic lipase extracts as enantioselective biocatalysts. Biotechnol Prog 20 (2004) 825-829
34. Turner N., Needs E., Khan J., and Vulfson E. Analysis of conformational states of Candida rugosa lipase in solution: implications for mechanism of interfacial activation and separation of open and closed forms. Biotechnol Bioeng 72 (2001) 108-118
35. Pernas M., López C., Rúa M.L., and Hermoso J. Influence of the conformational flexibility on the kinetics and dimerisation process of two Candida rugosa lipase isoenzymes. FEBS Lett 501 (2001) 87-91