Alkaline lipase from Pseudomonas fluorescens non-covalently immobilised on pristine versus oxidised multi-wall carbon nanotubes as efficient and recyclable catalytic systems in the synthesis of Solketal esters

Enzyme and Microbial Technology

Volumn 53, Issue 4, 2013, Pages 263-270

  Boncel, Sławomir ^a   Zniszczoł, Aurelia ^a   Szymańska, Katarzyna ^a   Mrowiec Białoń, Julita ^a,b   Jarzebski, Andrzej ^a   Walczak, Krzysztof Z ^a  

^a SILESIAN UNIVERSITY OF TECHNOLOGY   (Poland)

^b INSTITUTE OF CHEMICAL ENGINEERING   (Poland)

Author keywords

Alkaline lipase; Enantioselectivity; Immobilisation; Multi wall carbon nanotubes; Solketal esters; Transesterification

Indexed keywords

ALKALINE LIPASE; CHEMICAL FUNCTIONALISATION; COMPARATIVE STUDIES; ENANTIOSELECTIVE TRANSESTERIFICATION; HYDROPHOBIC INTERACTIONS; IMMOBILISATION; PSEUDOMONAS FLUORESCENS; TRANSESTERIFICATIONS;

ALKALINITY; BACTERIA; CATALYSTS; ENANTIOSELECTIVITY; ESTERIFICATION; ESTERS; INDUSTRIAL APPLICATIONS; MULTIWALLED CARBON NANOTUBES (MWCN); REUSABILITY; TRANSESTERIFICATION;

LIPASES;

ALKALINE LIPASE; ESTER DERIVATIVE; MULTI WALLED NANOTUBE; SILICON DIOXIDE; TRIACYLGLYCEROL LIPASE; UNCLASSIFIED DRUG;

ARTICLE; CATALYSIS; CATALYST; COMPARATIVE STUDY; ENANTIOSELECTIVITY; ENZYME IMMOBILIZATION; GAS CHROMATOGRAPHY; KINETICS; MORPHOLOGY; NONHUMAN; PSEUDOMONAS FLUORESCENS; SYNTHESIS; TRANSESTERIFICATION;

PSEUDOMONAS FLUORESCENS;

ALKALINE LIPASE; ENANTIOSELECTIVITY; IMMOBILISATION; MULTI-WALL CARBON NANOTUBES; SOLKETAL ESTERS; TRANSESTERIFICATION;

BACTERIAL PROTEINS; BIOCATALYSIS; BIOTECHNOLOGY; ENZYMES, IMMOBILIZED; ESTERIFICATION; ESTERS; HYDROGEN-ION CONCENTRATION; LIPASE; MICROSCOPY, ELECTRON; NANOTUBES, CARBON; OXIDATION-REDUCTION; PSEUDOMONAS FLUORESCENS; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; SPECTRUM ANALYSIS, RAMAN; STEREOISOMERISM;

EID: 84881546529     PISSN: 01410229     EISSN: 18790909     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2013.05.003     Document Type: Article

References (34)

1. Lowe D.A. Production of enzymes. Basic biotechnology 2001, 391-408. Cambridge University Press, Cambridge. C. Ratledge, B. Kristiansen (Eds.).
2. Tischer W., Wedekind F. Biocatalysis - from discovery to application - topics in current chemistry 1999, 200:96-111. Springer Verlag, Berlin; Heidelberg.
3. Monbaliu J.C., Winter M., Chevalier B., Schmidt F., Jiang Y., Hoogendoorn R., et al. Effective production of the biodiesel additive STBE by a continuous flow process. Bioresource Technology 2011, 102:9304-9307.
4. Li L., Korányi T.I., Sels B.F., Pescarmona P.P. Highly-efficient conversion of glycerol to solketal over heterogeneous Lewis acid catalysts. Green Chemistry 2012, 14:1611-1619.
5. Molinari F., Cavenago K.S., Romano A., Romano D., Gandolfi R. Enantioselective hydrolysis of (R,S)-isopropylideneglycerol acetate with Kluyveromyces marxianus. Tetrahedron: Asymmetry 2004, 15:1945-1947.
6. Hof R.P., Kellogg R.M. Synthesis and lipase-catalyzed resolution of 5-(hydroxymethyl)-1,3-dioxolan-4-ones: masked glycerol analogs as potential building blocks for pharmaceuticals. Journal of Organic Chemistry 1996, 61:3423-3427.
7. Hanson R.M. The synthetic methodology of nonracemic glycidol and related 2,3-epoxy alcohols. Chemical Reviews 1991, 91:437-475.
8. Singh C., Shaffer M., Koziol K., Kinloch I., Windle A. Towards the production of large-scale aligned carbon nanotubes. Chemical Physics Letters 2003, 372:860-865.
9. Jia G., Wang H., Yan L., Wang X., Pei R., Yan T., et al. Cytotoxicity of carbon nanomaterials: single-wall nanotube, multi-wall nanotube, and fullerene. Environmental Science and Technology 2005, 39:1378-1383.
10. Nikolaos K., Nikos T. Current progress on the chemical modification of carbon nanotubes. Chemical Reviews 2010, 110:5366-5397.
11. Shi J., Claussen J.C., McLamore E.S., Haque ul A., Jaroch D., Diggs A.R., et al. A comparative study of enzyme immobilization strategies for multi-walled carbon nanotube glucose biosensors. Nanotechnology 2011, 22:355502.
12. Feng W., Ji P. Enzymes immobilized on carbon nanotubes. Biotechnology Advances 2011, 29:889-895.
13. Shah S., Solanki K., Gupta M.N. Enhancement of lipase activity in non-aqueous media upon immobilization on multi-walled carbon nanotubes. Chemistry Central Journal 2007, 1:30.
14. Shi Q., Yang D., Su Y., Li J., Jiang Z., Jiang Y., et al. Covalent functionalization of multi-walled carbon nanotubes by lipase. Journal of Nanoparticle Research 2007, 9:1205-1210.
15. Tan H., Feng W., Ji P. Lipase immobilized on magnetic multi-walled carbon nanotubes. Bioresource Technology 2012, 115:172-176.
16. Ji P., Tan H., Xu X., Feng W. Lipase covalently attached to multiwalled carbon nanotubes as an efficient catalyst in organic solvent. AIChE Journal 2010, 56:3005-3011.
17. Kojima Y., Yokoe M., Mase T. Purification and partial characterization of an alkaline lipase from Pseudomonas pseudoalcaligenes F-111. Bioscience, Biotechnology, and Biochemistry 1994, 58:1564-1568.
18. Boncel S., Koziol K.K., Walczak K.Z., Windle A.H., Shaffer M.S. Infiltration of highly aligned carbon nanotube arrays with molten polystyrene. Materials Letters 2011, 65:2299-2303.
19. Lowry O.H., Rosebrough N.J., Lewis Farr A., Randall R.J. Protein measurement with the folin phenol reagent. Journal of Biological Chemistry 1951, 193:265-275.
20. Conde S., Corral C., Lissavetzky J. Analogs of propranolol. Synthesis of 3-alkylamino-1-(3-benzo[b]thienyloxy)-2-propanols. Journal of Heterocyclic Chemistry 1980, 17:937-940.
21. Schmid R.D., Verger R. Lipases: interfacial enzymes with attractive applications. Angewandte Chemie International Edition 1998, 37:1608-1633.
22. Boncel S., Walczak K.Z., Koziol K.K.K. Dynamics of capillary infiltration of liquids into a highly aligned multi-walled carbon nanotube film. Beilstein Journal of Nanotechnology 2011, 2:311-317.
23. Boncel S., Brzezinski M., Mrowiec-Bialon J., Janas D., Koziol K.K.K., Walczak K.Z. Oxidised multi-wall carbon nanotubes-(R)-polylactide composite with a covalent β-d-uridine filler-matrix linker. Materials Letters 2013, 91:50-54.
24. Boncel S., Müller K.H., Skepper J.N., Walczak K.Z., Koziol K.K.K. Tunable chemistry and morphology of multi-wall carbon nanotubes as a route to non-toxic, theranostic systems. Biomaterials 2011, 32:7677-7686.
25. Reichenbächer M., Popp J. Challenges in molecular structure determination 2012, Springer, Berlin; Heidelberg.
26. Chen C.-S., Fujimoto Y., Girdaukas G., Charles J.S. Quantitative analyses of biochemical kinetic resolutions of enantiomers. Journal of the American Chemical Society 1982, 104:7294-7299.
27. Machado A.C.O., da Silva A.A.T., Borges C.P., Simas A.B.C., Freire D.M.G. Kinetic resolution of (R,S)-1,2-isopropylidene glycerol (solketal) ester derivatives by lipases. Journal of Molecular Catalysis B: Enzymatic 2011, 69:42-46.
28. Berglund P. Controlling lipase enantioselectivity for organic synthesis. Biomolecular Engineering 2001, 18:13-22.
29. Wang Q., Zhou L., Jiang Y., Gao J. Improved stability of the carbon nanotubes-enzyme bioconjugates by biomimetic silicification. Enzyme and Microbial Technology 2011, 49:11-16.
30. Koziol K.K.K., Ducati C., Windle A.H. Carbon nanotubes with catalyst controlled chiral angle. Chemistry of Materials 2010, 22:4904-4911.
31. Peigney A., Laurent C., Flahaut E., Basca R.R., Rousset A. Specific surface area of carbon nanotubes and bundles of carbon nanotubes. Carbon 2001, 39:507-514.
32. Lehman J.H., Terrones M., Mansfield E., Hurst K.E., Meunier V. Evaluating the characteristics of multiwall carbon nanotubes. Carbon 2011, 49:2581-2602.
33. Bordes F., Barbe S., Escalier P., Mourey L., Andre I., Marty A., et al. Exploring the conformational states and rearrangements of Yarrowia lipolytica lipase. Biophysical Journal 2010, 99:2225-2234.
34. Feng W., Sun X., Ji P. Activation mechanism of Yarrowia lipolytica lipase immobilized on carbon nanotubes. Soft Matter 2012, 8:7143-7150.