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Journal
2014 | 12 | 12 | 1262-1270
Article title

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

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EN
Abstracts
EN
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).
Publisher
Journal
Year
Volume
12
Issue
12
Pages
1262-1270
Physical description
Dates
published
1 - 12 - 2014
online
7 - 6 - 2014
References
  • [1] P. Grunwald, Biocatalysis. Biochemical Fundaments and Applications (Imperial College Press, London, 2011)
  • [2] P. Seufer-Wasserthal, Pharm. Tech. October, 53 (2010)
  • [3] R.A. Sheldon, Org. Process Res. Dev. 15, 213 (2011) http://dx.doi.org/10.1021/op100289f[Crossref]
  • [4] A.S. Bommarius, B.R. Riebel, Biocatalysis, (Wiley-VCH Verlag GmbH&Co. KGaA, Weinheim, 2004) http://dx.doi.org/10.1002/3527602364[Crossref]
  • [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.2011.01.007[Crossref]
  • [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.2007.01.018[Crossref]
  • [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)00224-2[Crossref]
  • [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.2004.09.013[Crossref]
  • [9] R. Fernandez-Lafuente, J. Mol. Catal. B: Enzym. 62, 197 (2010) http://dx.doi.org/10.1016/j.molcatb.2009.11.010[Crossref]
  • [10] G. Bayramoglu, B. Kaya, M.Y. Arica, Food Chem. 92, 261 (2005) http://dx.doi.org/10.1016/j.foodchem.2004.07.022[Crossref]
  • [11] R.A. Sheldon, Appl. Microbiol. Biot. 92, 467 (2011) http://dx.doi.org/10.1007/s00253-011-3554-2[Crossref]
  • [12] M.M.M. Elnashar, J. Biomat. Nanobiot. 1, 61 (2010) http://dx.doi.org/10.4236/jbnb.2010.11008[Crossref]
  • [13] M. Tudorache, A. Nae, S. Coman, V.I. Parvulescu, RSC Adv. 3, 4052 (2013) http://dx.doi.org/10.1039/c3ra23222k[Crossref]
  • [14] M. Aresta, A. Dibenedetto, F. Nocito, C. Ferragina, J. Catal. 268, 106 (2009) http://dx.doi.org/10.1016/j.jcat.2009.09.008[Crossref]
  • [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.2010.03.009[Crossref]
  • [16] A. Behr, J. Eilting, K. Irawadi, J. Leschinski. F. Lindner, Green Chem. 10, 13 (2008) http://dx.doi.org/10.1039/b710561d[Crossref]
  • [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.2007.08.007[Crossref]
  • [18] E.Y. Lee, K.H. Lee, C.-H. Park, Bioproc. Biosys. Eng. 33, 1059 (2010) http://dx.doi.org/10.1007/s00449-010-0431-9[Crossref]
  • [19] M. Tudorache, L. Protesescu, S. Coman. V.I. Parvulescu, Green Chem. 14, 478 (2012) http://dx.doi.org/10.1039/c2gc16294f[Crossref]
  • [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.2013.02.049[Crossref]
  • [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.2012.06.016[Crossref]
Document Type
Publication order reference
YADDA identifier
bwmeta1.element.-psjd-doi-10_2478_s11532-014-0547-x
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