Skip to content
BY-NC-ND 3.0 license Open Access Published by De Gruyter Open Access June 7, 2014

Biocatalytic designs for the conversion of renewable glycerol into glycerol carbonate as a value-added product

  • Madalina Tudorache EMAIL logo , George Ghemes , Andreea Nae , Elena Matei , Ionel Mercioniu , Erhard Kemnitz , Benjamin Ritter , Simona Coman and Vasile Parvulescu
From the journal Open Chemistry

Abstract

A comparative study of two different biocatalytic models, e.g. enzyme immobilized on magnetic particles (EIMP) and cross-linking enzyme aggregates onto magnetic particles (CLEMPA) was performed. The first model was designed as enzyme-immobilized on the magnetic particles surface (EIMP). The second model was constructed as a network structure with the enzyme aggregates and magnetic particles placed into the nodes and polyglutaraldehyde cross-linker as the network ledges. The design was called cross-linking enzyme aggregates onto magnetic particles (CLEMPA). The biocatalysts were prepared using lipase enzyme from Aspergillus niger for catalyzing the glycerol (Gly) conversion to glycerol carbonate (GlyC). The biocatalyst characteristics for both designs (EIMP and CLEMPA) were evaluated using scanning electron microscopy (SEM), laser light scattering (LLS) and UV-Vis techniques. The EIMP model was strongly influenced by the composition of the polymeric layer covering the particles surface, while the size of the magnetic particles affected mostly the CLEMPA design. Also, the biocatalytic capacity of the tested models was evaluated as maximum 52% Gly conversion with 90% GlyC selectivity for EIMP, and 73% Gly conversion with 77% GlyC selectivity for CLEMPA. Both biocatalytic models were successfully used to prepare GlyC from “crude” glycerol collected directly from the biodiesel process (e.g. 49% Gly conversion with 91% GlyC selectivity for EIMP and 70% Gly conversion with 80% GlyC selectivity for CLEMPA).

[1] P. Grunwald, Biocatalysis. Biochemical Fundaments and Applications (Imperial College Press, London, 2011) Search in Google Scholar

[2] P. Seufer-Wasserthal, Pharm. Tech. October, 53 (2010) Search in Google Scholar

[3] R.A. Sheldon, Org. Process Res. Dev. 15, 213 (2011) http://dx.doi.org/10.1021/op100289f10.1021/op100289fSearch in Google Scholar

[4] A.S. Bommarius, B.R. Riebel, Biocatalysis, (Wiley-VCH Verlag GmbH&Co. KGaA, Weinheim, 2004) http://dx.doi.org/10.1002/352760236410.1002/3527602364Search in Google Scholar

[5] M. Tudorache, D. Mahalu, C. Teodorescu, R. Stan, C. Bala, V.I. Parvulescu, J. Mol. Catal. B: Enzym. 69, 133 (2011) http://dx.doi.org/10.1016/j.molcatb.2011.01.00710.1016/j.molcatb.2011.01.007Search in Google Scholar

[6] C. Mateo, J.M. Palomo, G. Fernandez-Lorente, J.M. DGuisan, R. Fernandez-Lafuente, Enzyme Microb. Tech. 40, 1451 (2007) http://dx.doi.org/10.1016/j.enzmictec.2007.01.01810.1016/j.enzmictec.2007.01.018Search in Google Scholar

[7] J.M. Palomo, G. Muñoz, G. Fernández-Lorente. C. Mateo, M. Fuentes, J.M. Guisan. R. Fernández-Lafuente, J. Mol. Catal B: Enzym. 21, 201 (2003) http://dx.doi.org/10.1016/S1381-1177(02)00224-210.1016/S1381-1177(02)00224-2Search in Google Scholar

[8] J.M. Palomo, C. Ortiz, G. Fernández-Lorente. M. Fuentes, J.M. Guisán, R. Fernández-Lafuente, Enzyme Microb. Tech. 36, 447 (2005) http://dx.doi.org/10.1016/j.enzmictec.2004.09.01310.1016/j.enzmictec.2004.09.013Search in Google Scholar

[9] R. Fernandez-Lafuente, J. Mol. Catal. B: Enzym. 62, 197 (2010) http://dx.doi.org/10.1016/j.molcatb.2009.11.01010.1016/j.molcatb.2009.11.010Search in Google Scholar

[10] G. Bayramoglu, B. Kaya, M.Y. Arica, Food Chem. 92, 261 (2005) http://dx.doi.org/10.1016/j.foodchem.2004.07.02210.1016/j.foodchem.2004.07.022Search in Google Scholar

[11] R.A. Sheldon, Appl. Microbiol. Biot. 92, 467 (2011) http://dx.doi.org/10.1007/s00253-011-3554-210.1007/s00253-011-3554-2Search in Google Scholar PubMed PubMed Central

[12] M.M.M. Elnashar, J. Biomat. Nanobiot. 1, 61 (2010) http://dx.doi.org/10.4236/jbnb.2010.1100810.4236/jbnb.2010.11008Search in Google Scholar

[13] M. Tudorache, A. Nae, S. Coman, V.I. Parvulescu, RSC Adv. 3, 4052 (2013) http://dx.doi.org/10.1039/c3ra23222k10.1039/c3ra23222kSearch in Google Scholar

[14] M. Aresta, A. Dibenedetto, F. Nocito, C. Ferragina, J. Catal. 268, 106 (2009) http://dx.doi.org/10.1016/j.jcat.2009.09.00810.1016/j.jcat.2009.09.008Search in Google Scholar

[15] C. Magniont, G. Escadeillas, C. Oms-Multon. P. De Caro, Cement Concrete Res. 40, 1072 (2010) http://dx.doi.org/10.1016/j.cemconres.2010.03.00910.1016/j.cemconres.2010.03.009Search in Google Scholar

[16] A. Behr, J. Eilting, K. Irawadi, J. Leschinski. F. Lindner, Green Chem. 10, 13 (2008) http://dx.doi.org/10.1039/b710561d10.1039/B710561DSearch in Google Scholar

[17] S.C. Kim, Y.H. Kim, H. Lee, D.Y. Yoon, B.K. Song, J. Mol. Catal. B: Enzym. 49, 75 (2007) http://dx.doi.org/10.1016/j.molcatb.2007.08.00710.1016/j.molcatb.2007.08.007Search in Google Scholar

[18] E.Y. Lee, K.H. Lee, C.-H. Park, Bioproc. Biosys. Eng. 33, 1059 (2010) http://dx.doi.org/10.1007/s00449-010-0431-910.1007/s00449-010-0431-9Search in Google Scholar PubMed

[19] M. Tudorache, L. Protesescu, S. Coman. V.I. Parvulescu, Green Chem. 14, 478 (2012) http://dx.doi.org/10.1039/c2gc16294f10.1039/c2gc16294fSearch in Google Scholar

[20] M. Tudorache, A. Negoi, B. Tudora, V.I. Parvulescu, Appl. Catal. B-Environ. 146, 274 (2014) http://dx.doi.org/10.1016/j.apcatb.2013.02.04910.1016/j.apcatb.2013.02.049Search in Google Scholar

[21] M. Tudorache, L. Protesescu, A. Negi. V.I. Parvulescu, Appl. Catal. A-Gen. 437–438, 90 (2012) http://dx.doi.org/10.1016/j.apcata.2012.06.01610.1016/j.apcata.2012.06.016Search in Google Scholar

Published Online: 2014-6-7
Published in Print: 2014-12-1

© 2014 Versita Warsaw

This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 3.0 License.

Downloaded on 27.9.2023 from https://www.degruyter.com/document/doi/10.2478/s11532-014-0547-x/html
Scroll to top button