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Fermentation 2018, 4(3), 75; https://doi.org/10.3390/fermentation4030075

Effect of Operating Variables and Kinetics of the Lipase Catalyzed Transesterification of Ethylene Carbonate and Glycerol

1
Department of Materials & Chemical Engineering, Chemical Sciences College, Complutense University of Madrid, 28040 Madrid, Spain
2
Chemical Engineering Pilot Plant (PLAPIQUI), Scientific and Technological Centre, Universidad Nacional del Sur-CONICET, 8000 Bahia Blanca, Argentina
3
Molecular Catalysis Division, Max Planck Institute for Chemical Energy Conversion, Stiftstrasse 34–36, 45470 Mülheim an der Ruhr, Germany
*
Author to whom correspondence should be addressed.
Received: 4 July 2018 / Revised: 12 August 2018 / Accepted: 2 September 2018 / Published: 5 September 2018
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Abstract

Glycerol carbonate (GC) is a value-added product originating from the valorization of widely available glycerol (Gly), a side stream from the production of biodiesel. Here we approach the production of this chemical comparing two reactions based on the transesterification of Gly with dimethyl carbonate (DMC) and ethylene carbonate (EC). When using DMC, it was observed that the free enzyme CALB (lipase B from Candida antarctica) gave the best results, whereas Eversa Transform (a genetic modification of Thermomyces lanuginosus lipase) performed better than the rest if EC was the reagent. With the selected catalysts, their immobilized analogous enzymes Novozym 435 and Lypozyme TL IM, respectively, were also tested. Observing that the yields for the reaction with EC were significantly faster, other operating variables were evaluated, resulting the best performance using a closed system, tert-butanol as solvent, a concentration of enzyme Eversa Transform of 3% w/w, a molar excess of EC:Gly of 9:1 and a temperature of 60 °C. Finally, several runs were conducted at different temperatures and molar ratios of EC:Gly, fitting a kinetic model to all experimental data for the reaction catalyzed with Eversa Transform. This model included the bimolecular transesterification reaction of Gly and EC catalyzed by the lipase and a reversible ring-opening polymerization of EC. View Full-Text
Keywords: glycerol; glycerol carbonate; Novozym 435; Lipozyme TL 100 L; Eversa Transform 2.0; kinetic model glycerol; glycerol carbonate; Novozym 435; Lipozyme TL 100 L; Eversa Transform 2.0; kinetic model
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).
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Gutierrez-Lazaro, A.; Velasco, D.; Boldrini, D.E.; Yustos, P.; Esteban, J.; Ladero, M. Effect of Operating Variables and Kinetics of the Lipase Catalyzed Transesterification of Ethylene Carbonate and Glycerol. Fermentation 2018, 4, 75.

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