Kinetics of Enantiomerically Enriched Synthesis of Solketal Esters Using Native and SBA-15 supported P. Fluorescens Lipase

• Autorzy: Zniszczoł A. , Szymańska K. , Kocurek J. , Bryjak J. , Walczak K. , Jarzębski A.

Identyfikatory

DOI

10.1515/cpe-2017-0016

• Języki publikacji: EN

Abstrakty

EN

The studies showed that alkaline lipase from Pseudomonas fluorescens enables an irreversible transesterification of vinyl esters to give enantiomeric excess (eeR) of about 80% using vinyl butyrate as acyl donor and diisopropyl ether as a solvent, at partially optimized conditions. For the native lipase the process was adequately described by a five-parameter Ping-Pong Bi Bi model for both enantiomers plus expression accounting for the formation of enzyme-acyl donor complex, but for the same lipase supported on mesoporous materials of SBA-15-Oc type, R-product inhibition also had to be taken into account. The use of hydrophobic support increased by more than two-fold the rate of the S-solketal conversion but even more that of R-solketal. Thus the immobilization of lipase had very positive effect on the process kinetics but decreased its enantioselectivity.

Słowa kluczowe

EN

bioenantioselectivity; solketal; ping-pong kinetics; transesterification

PL

kinetyka ping-ponga; transestryfikacja

• Wydawca: Komitet Inżynierii Chemicznej i Procesowej Polskiej Akademii Nauk
• Czasopismo: Chemical and Process Engineering
• Rocznik: 2017
• Tom: Vol. 38, nr 2
• Strony: 209--215
• Opis fizyczny: Bibliogr. 11 poz., rys., tab.

Twórcy

autor

Zniszczoł A.

• Department of Chemical Engineering and Process Design, Silesian University of Technology, 44-100 Gliwice, Ks. M. Strzody 7, Poland

autor

Szymańska K.

• Department of Chemical Engineering and Process Design, Silesian University of Technology, 44-100 Gliwice, Ks. M. Strzody 7, Poland

autor

Kocurek J.

• Department of Chemical Engineering and Process Design, Silesian University of Technology, 44-100 Gliwice, Ks. M. Strzody 7, Poland

autor

Bryjak J.

• Department of Bioroganic Chemistry, Faculty of Chemistry, Wrocław University of Technology, 50-370 Wrocław, Wybrzeże Wyspiańskiego 27, Poland

autor

Walczak K.

• Department of Chemical Engineering and Process Design, Silesian University of Technology, 44-100 Gliwice, Ks. M. Strzody 7, Poland

autor

Jarzębski A.

• Department of Chemical Engineering and Process Design, Silesian University of Technology, 44-100 Gliwice, Ks. M. Strzody 7, Poland
• Department of Bioroganic Chemistry, Faculty of Chemistry, Wrocław University of Technology, 50-370 Wrocław, Wybrzeże Wyspiańskiego 27, Poland

Bibliografia

• 1. Adlercreutz P., 2013. Immobilization and application of lipases in organic media. Chem. Soc. Rev., 42, 6406-6436. DOI: 10.1039/c3cs35446f.
• 2. Barros D.P.C., Lemos F., Fonseca L.P., Cabral J.M.S., 2010. Kinetic cutinase-catalyzed esterification of caproic acid in organic solvent system. J. Mol. Catal. B: Enzym., 66, 285-293. DOI: 10.1016/j.molcatb.2010.06.005.
• 3. Boncel S., Zniszczoł A., Szymańska K., Mrowiec-Białoń J., Jarzębski A., Walczak K., 2013. 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 Microb. Technol., 53, 263-270. DOI: 10.1016/j.enzmictec.2013.05.003.
• 4. Hanson R.M., 1991. The synthetic methodology of nonracemic glycidol and related 2,3-epoxy alcohols. Chem. Rev., 91, 437-475. DOI: 10.1021/cr00004a001.
• 5. Hof R.P., Kellog R.M., 1996. Synthesis and lipase-catalyzed resolution of 5-(hydroxymethyl)-1,3-dioxolan-4- ones: Masked glycerol analogs as potential building blocks for pharmaceuticals. J. Org. Chem., 61, 3423-3427. DOI: 10.1021/jo952021v.
• 6. Hydziuszko Z., Dmytryk A., Majewska P., Szymańska K., Liesiena J., Jarzębski A., Bryjak J., 2014. Screening of lipase carriers for reactions in water, biphasic and pure organic solvent systems. Acta Biochim. Polonica, 61(1), 1-6.
• 7. Majewska P., Kafarski P., Lejczak B., 2006. Simple and effective method for the deracemization of ethyl-1- hydroxyphosphinate using biocatalysts with lipolitic activity. Tetrahedron Asymmetry, 17, 2870-2875. DOI: 10.1016/j.tetasy.2006.10.041.
• 8. Paiva A.L., Balcao V.M., Malcata F.X., 2000. Kinetics and mechanisms of reactions catalyzed by immobilized lipases. Enzyme Microb. Technol., 27, 187-204. DOI: 10.1016/S0141-0229(00)00206-4.
• 9. Pilarek M., Szewczyk K.W., 2007. Kinetic model of 1,3-specific triacylglycerols alcoholysis catalyzed by lipases. J. Biotechnol., 127, 736-744. DOI: 10.1016/j.jbiotec.2006.08.012.
• 10. Zniszczoł A., 2015. Otrzymywanie estrów solketalu wobec lipaz natywnych oraz immobilizowanych na nośnikach stałych. Ph.D. thesis, Silesian University of Technology, Gliwice.
• 11. Zniszczoł A., Herman A.P., Szymańska K., Mrowiec-Białoń J., Walczak K., Jarzębski A., Boncel S., 2016. Covalently immobilized lipase on aminoalkyl-, carboxy- and hydroxy-multi-wall carbon nanotubes in the enantioselective synthesis of solketal esters. Enzyme Microb. Technol., 87, 61-69. DOI: 10.1016/j.enzmictec.2016.02.015.

Uwagi

PL

Opracowanie ze środków MNiSW w ramach umowy 812/P-DUN/2016 na działalność upowszechniającą naukę (zadania 2017)