Novel Combi-lipase Systems for Fatty Acid Ethyl Esters Production
Most Combi-lipases (CL) are based on mixtures of different lipases immobilized on different supports. The increased CL efficiency has been attributed solely to the complementary selectivity of lipases. However, the role of the immobilization support in CL or in co-immobilized systems ( co CL) and th...
Published in: | Catalysts |
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Language: | English |
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MDPI AG
2019
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Online Access: | https://doi.org/10.3390/catal9060546 https://doaj.org/article/bfe16dc4aa0142f1865b8b1b8fc9fc45 |
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author | Esteban C. Toro Diego F. Rodríguez Nelson Morales Lina M. García César A. Godoy |
author_facet | Esteban C. Toro Diego F. Rodríguez Nelson Morales Lina M. García César A. Godoy |
author_sort | Esteban C. Toro |
collection | Directory of Open Access Journals: DOAJ Articles |
container_issue | 6 |
container_start_page | 546 |
container_title | Catalysts |
container_volume | 9 |
description | Most Combi-lipases (CL) are based on mixtures of different lipases immobilized on different supports. The increased CL efficiency has been attributed solely to the complementary selectivity of lipases. However, the role of the immobilization support in CL or in co-immobilized systems ( co CL) and the application of kinetic models to account CL composition effects, have not been assessed. In this work, commercial lipases from Thermomyces lunuginosus (TLL), Candida antarctica (CALB) and Rhizomocur miehei (RML) and supports as Lewatit ® VPOC1600 (LW) and Purolite ® ECR1604 (PU), were combined to produce new CL systems for the production of fatty acid ethyl esters (EE) which are the main component of ethylic biodiesel: Co -immobilization slightly altered palm olein EE yields with regard to that of equivalent CL systems, e.g., the best co CL of TLL and CALB in LW (89.5%) and the respective CL (81.8%). The support did affect CL behavior: (i) The best co CL of TLL and RML on LW produced 80.0% EE while on PU 76.4%; (ii) CL based on mixtures of the same enzyme, but immobilized on different supports ( semi CL) show complementarity: The best TLL semi CL produced 86.1% EE while its constituents (LW) and (PU) produced individually 78.2 and 70.3%, respectively. The proposed model accounts adequately the EE production properties for CL systems based on TLL, CALB and LW. This work expands the tools to obtain new CL systems for EE production. |
format | Article in Journal/Newspaper |
genre | Antarc* Antarctica |
genre_facet | Antarc* Antarctica |
id | ftdoajarticles:oai:doaj.org/article:bfe16dc4aa0142f1865b8b1b8fc9fc45 |
institution | Open Polar |
language | English |
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op_doi | https://doi.org/10.3390/catal9060546 |
op_relation | https://www.mdpi.com/2073-4344/9/6/546 https://doaj.org/toc/2073-4344 doi:10.3390/catal9060546 https://doaj.org/article/bfe16dc4aa0142f1865b8b1b8fc9fc45 |
op_source | Catalysts, Vol 9, Iss 6, p 546 (2019) |
publishDate | 2019 |
publisher | MDPI AG |
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spelling | ftdoajarticles:oai:doaj.org/article:bfe16dc4aa0142f1865b8b1b8fc9fc45 2025-01-16T19:05:50+00:00 Novel Combi-lipase Systems for Fatty Acid Ethyl Esters Production Esteban C. Toro Diego F. Rodríguez Nelson Morales Lina M. García César A. Godoy 2019-06-01T00:00:00Z https://doi.org/10.3390/catal9060546 https://doaj.org/article/bfe16dc4aa0142f1865b8b1b8fc9fc45 EN eng MDPI AG https://www.mdpi.com/2073-4344/9/6/546 https://doaj.org/toc/2073-4344 doi:10.3390/catal9060546 https://doaj.org/article/bfe16dc4aa0142f1865b8b1b8fc9fc45 Catalysts, Vol 9, Iss 6, p 546 (2019) immobilization Combi-lipases support biodiesel lipases transesterification Chemical technology TP1-1185 Chemistry QD1-999 article 2019 ftdoajarticles https://doi.org/10.3390/catal9060546 2024-09-25T15:39:09Z Most Combi-lipases (CL) are based on mixtures of different lipases immobilized on different supports. The increased CL efficiency has been attributed solely to the complementary selectivity of lipases. However, the role of the immobilization support in CL or in co-immobilized systems ( co CL) and the application of kinetic models to account CL composition effects, have not been assessed. In this work, commercial lipases from Thermomyces lunuginosus (TLL), Candida antarctica (CALB) and Rhizomocur miehei (RML) and supports as Lewatit ® VPOC1600 (LW) and Purolite ® ECR1604 (PU), were combined to produce new CL systems for the production of fatty acid ethyl esters (EE) which are the main component of ethylic biodiesel: Co -immobilization slightly altered palm olein EE yields with regard to that of equivalent CL systems, e.g., the best co CL of TLL and CALB in LW (89.5%) and the respective CL (81.8%). The support did affect CL behavior: (i) The best co CL of TLL and RML on LW produced 80.0% EE while on PU 76.4%; (ii) CL based on mixtures of the same enzyme, but immobilized on different supports ( semi CL) show complementarity: The best TLL semi CL produced 86.1% EE while its constituents (LW) and (PU) produced individually 78.2 and 70.3%, respectively. The proposed model accounts adequately the EE production properties for CL systems based on TLL, CALB and LW. This work expands the tools to obtain new CL systems for EE production. Article in Journal/Newspaper Antarc* Antarctica Directory of Open Access Journals: DOAJ Articles Catalysts 9 6 546 |
spellingShingle | immobilization Combi-lipases support biodiesel lipases transesterification Chemical technology TP1-1185 Chemistry QD1-999 Esteban C. Toro Diego F. Rodríguez Nelson Morales Lina M. García César A. Godoy Novel Combi-lipase Systems for Fatty Acid Ethyl Esters Production |
title | Novel Combi-lipase Systems for Fatty Acid Ethyl Esters Production |
title_full | Novel Combi-lipase Systems for Fatty Acid Ethyl Esters Production |
title_fullStr | Novel Combi-lipase Systems for Fatty Acid Ethyl Esters Production |
title_full_unstemmed | Novel Combi-lipase Systems for Fatty Acid Ethyl Esters Production |
title_short | Novel Combi-lipase Systems for Fatty Acid Ethyl Esters Production |
title_sort | novel combi-lipase systems for fatty acid ethyl esters production |
topic | immobilization Combi-lipases support biodiesel lipases transesterification Chemical technology TP1-1185 Chemistry QD1-999 |
topic_facet | immobilization Combi-lipases support biodiesel lipases transesterification Chemical technology TP1-1185 Chemistry QD1-999 |
url | https://doi.org/10.3390/catal9060546 https://doaj.org/article/bfe16dc4aa0142f1865b8b1b8fc9fc45 |