Potential new biocatalysts for biofuel production: The fungal lipases of Thermomyces lanuginosus and Rhizomucor miehei immobilized on zeolitic supports ion exchanged with transition metals
Autor(a) principal: | |
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Data de Publicação: | 2015 |
Outros Autores: | , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNESP |
Texto Completo: | http://dx.doi.org/10.1016/j.micromeso.2015.05.007 http://hdl.handle.net/11449/160651 |
Resumo: | Nanozeolite NaX ion exchanged with different transition metals (Mn2+,Cu2+, Co2+, Zn2+, Ni2+) was used as a solid support for the immobilization of the lipases of Thermomyces lanuginosus (TLL) and Rhizomucor miehei (RML). The nanozeolite-enzyme complexes were used as heterogeneous catalysts for the transesterification reaction of palm oil to fatty acid ethyl esters (FAEEs). The most relevant results were obtained with the T lanuginosus enzyme immobilized on nanozeolitic supports ion exchanged with Ni2+. Although these zeolitic supports were able to immobilize a relatively small amount of the enzyme (43.7%) in comparison with the other nanozeolitic supports, the FAEE yields obtained with Nano-X/Ni/0.5 M-TLL complexes were above 94%. These results revealed an unusual synergistic effect between the T lanuginosus enzyme and the nickel ion-exchanged nanozeolitic support; this effect was not observed for the complexes prepared with the R. miehei enzyme. Bioinformatics calculations were performed for both enzymes by taking into consideration the crystallographic structures of the enzymes and the zeta potential of the surface of the nanozeolitic supports. By combining calculations of the protein electrostatic potential surface and normal mode analyses in a model, we were able to propose an explanation for the synergistic effect between the lipases and the nanozeolitic supports. The synergistic effect could be explained through an allosteric mechanism describing the interaction between aspartic acid residues 102 and 158 of the T lanuginosus lipase and the positively charged zeolitic support surface. This interaction results in the stabilization of the opening of the enzyme lid and leaves its catalytic triad permanently exposed to the reaction medium. (C) 2015 Elsevier Inc. All rights reserved. |
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Potential new biocatalysts for biofuel production: The fungal lipases of Thermomyces lanuginosus and Rhizomucor miehei immobilized on zeolitic supports ion exchanged with transition metalsZeolite-enzyme interactionBioinformatic calculationsBiomassBiofuelsNanozeolite NaX ion exchanged with different transition metals (Mn2+,Cu2+, Co2+, Zn2+, Ni2+) was used as a solid support for the immobilization of the lipases of Thermomyces lanuginosus (TLL) and Rhizomucor miehei (RML). The nanozeolite-enzyme complexes were used as heterogeneous catalysts for the transesterification reaction of palm oil to fatty acid ethyl esters (FAEEs). The most relevant results were obtained with the T lanuginosus enzyme immobilized on nanozeolitic supports ion exchanged with Ni2+. Although these zeolitic supports were able to immobilize a relatively small amount of the enzyme (43.7%) in comparison with the other nanozeolitic supports, the FAEE yields obtained with Nano-X/Ni/0.5 M-TLL complexes were above 94%. These results revealed an unusual synergistic effect between the T lanuginosus enzyme and the nickel ion-exchanged nanozeolitic support; this effect was not observed for the complexes prepared with the R. miehei enzyme. Bioinformatics calculations were performed for both enzymes by taking into consideration the crystallographic structures of the enzymes and the zeta potential of the surface of the nanozeolitic supports. By combining calculations of the protein electrostatic potential surface and normal mode analyses in a model, we were able to propose an explanation for the synergistic effect between the lipases and the nanozeolitic supports. The synergistic effect could be explained through an allosteric mechanism describing the interaction between aspartic acid residues 102 and 158 of the T lanuginosus lipase and the positively charged zeolitic support surface. This interaction results in the stabilization of the opening of the enzyme lid and leaves its catalytic triad permanently exposed to the reaction medium. (C) 2015 Elsevier Inc. All rights reserved.Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)Univ Estadual Paulista, UNESP, Dept Fis, Inst Biociencias Letras & Ciencias Exatas, BR-15054000 Sao Paulo, BrazilUniv Fed Rio de Janeiro, Lab Greentec, Escola Quim, BR-21945970 Rio De Janeiro, RJ, BrazilUniv Estadual Paulista, UNESP, Dept Fis, Inst Biociencias Letras & Ciencias Exatas, BR-15054000 Sao Paulo, BrazilFAPESP: 11/51851-5FAPESP: 11/10092-4CNPq: 406761/2013-2Elsevier B.V.Universidade Estadual Paulista (Unesp)Universidade Federal do Rio de Janeiro (UFRJ)Vasconcellos, Adriano de [UNESP]Laurenti, Juliana Bergamasco [UNESP]Miller, Alex Henrique [UNESP]Silva, Danilo Antonio da [UNESP]Moraes, Fabio Rogerio de [UNESP]Aranda, Donato A. G.Nery, Jose G. [UNESP]2018-11-26T16:16:09Z2018-11-26T16:16:09Z2015-09-15info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article166-180application/pdfhttp://dx.doi.org/10.1016/j.micromeso.2015.05.007Microporous And Mesoporous Materials. Amsterdam: Elsevier Science Bv, v. 214, p. 166-180, 2015.1387-1811http://hdl.handle.net/11449/16065110.1016/j.micromeso.2015.05.007WOS:000356749900023WOS000356749900023.pdfWeb of Sciencereponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengMicroporous And Mesoporous Materials1,080info:eu-repo/semantics/openAccess2024-01-27T07:01:07Zoai:repositorio.unesp.br:11449/160651Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-06T00:06:51.948229Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
dc.title.none.fl_str_mv |
Potential new biocatalysts for biofuel production: The fungal lipases of Thermomyces lanuginosus and Rhizomucor miehei immobilized on zeolitic supports ion exchanged with transition metals |
title |
Potential new biocatalysts for biofuel production: The fungal lipases of Thermomyces lanuginosus and Rhizomucor miehei immobilized on zeolitic supports ion exchanged with transition metals |
spellingShingle |
Potential new biocatalysts for biofuel production: The fungal lipases of Thermomyces lanuginosus and Rhizomucor miehei immobilized on zeolitic supports ion exchanged with transition metals Vasconcellos, Adriano de [UNESP] Zeolite-enzyme interaction Bioinformatic calculations Biomass Biofuels |
title_short |
Potential new biocatalysts for biofuel production: The fungal lipases of Thermomyces lanuginosus and Rhizomucor miehei immobilized on zeolitic supports ion exchanged with transition metals |
title_full |
Potential new biocatalysts for biofuel production: The fungal lipases of Thermomyces lanuginosus and Rhizomucor miehei immobilized on zeolitic supports ion exchanged with transition metals |
title_fullStr |
Potential new biocatalysts for biofuel production: The fungal lipases of Thermomyces lanuginosus and Rhizomucor miehei immobilized on zeolitic supports ion exchanged with transition metals |
title_full_unstemmed |
Potential new biocatalysts for biofuel production: The fungal lipases of Thermomyces lanuginosus and Rhizomucor miehei immobilized on zeolitic supports ion exchanged with transition metals |
title_sort |
Potential new biocatalysts for biofuel production: The fungal lipases of Thermomyces lanuginosus and Rhizomucor miehei immobilized on zeolitic supports ion exchanged with transition metals |
author |
Vasconcellos, Adriano de [UNESP] |
author_facet |
Vasconcellos, Adriano de [UNESP] Laurenti, Juliana Bergamasco [UNESP] Miller, Alex Henrique [UNESP] Silva, Danilo Antonio da [UNESP] Moraes, Fabio Rogerio de [UNESP] Aranda, Donato A. G. Nery, Jose G. [UNESP] |
author_role |
author |
author2 |
Laurenti, Juliana Bergamasco [UNESP] Miller, Alex Henrique [UNESP] Silva, Danilo Antonio da [UNESP] Moraes, Fabio Rogerio de [UNESP] Aranda, Donato A. G. Nery, Jose G. [UNESP] |
author2_role |
author author author author author author |
dc.contributor.none.fl_str_mv |
Universidade Estadual Paulista (Unesp) Universidade Federal do Rio de Janeiro (UFRJ) |
dc.contributor.author.fl_str_mv |
Vasconcellos, Adriano de [UNESP] Laurenti, Juliana Bergamasco [UNESP] Miller, Alex Henrique [UNESP] Silva, Danilo Antonio da [UNESP] Moraes, Fabio Rogerio de [UNESP] Aranda, Donato A. G. Nery, Jose G. [UNESP] |
dc.subject.por.fl_str_mv |
Zeolite-enzyme interaction Bioinformatic calculations Biomass Biofuels |
topic |
Zeolite-enzyme interaction Bioinformatic calculations Biomass Biofuels |
description |
Nanozeolite NaX ion exchanged with different transition metals (Mn2+,Cu2+, Co2+, Zn2+, Ni2+) was used as a solid support for the immobilization of the lipases of Thermomyces lanuginosus (TLL) and Rhizomucor miehei (RML). The nanozeolite-enzyme complexes were used as heterogeneous catalysts for the transesterification reaction of palm oil to fatty acid ethyl esters (FAEEs). The most relevant results were obtained with the T lanuginosus enzyme immobilized on nanozeolitic supports ion exchanged with Ni2+. Although these zeolitic supports were able to immobilize a relatively small amount of the enzyme (43.7%) in comparison with the other nanozeolitic supports, the FAEE yields obtained with Nano-X/Ni/0.5 M-TLL complexes were above 94%. These results revealed an unusual synergistic effect between the T lanuginosus enzyme and the nickel ion-exchanged nanozeolitic support; this effect was not observed for the complexes prepared with the R. miehei enzyme. Bioinformatics calculations were performed for both enzymes by taking into consideration the crystallographic structures of the enzymes and the zeta potential of the surface of the nanozeolitic supports. By combining calculations of the protein electrostatic potential surface and normal mode analyses in a model, we were able to propose an explanation for the synergistic effect between the lipases and the nanozeolitic supports. The synergistic effect could be explained through an allosteric mechanism describing the interaction between aspartic acid residues 102 and 158 of the T lanuginosus lipase and the positively charged zeolitic support surface. This interaction results in the stabilization of the opening of the enzyme lid and leaves its catalytic triad permanently exposed to the reaction medium. (C) 2015 Elsevier Inc. All rights reserved. |
publishDate |
2015 |
dc.date.none.fl_str_mv |
2015-09-15 2018-11-26T16:16:09Z 2018-11-26T16:16:09Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://dx.doi.org/10.1016/j.micromeso.2015.05.007 Microporous And Mesoporous Materials. Amsterdam: Elsevier Science Bv, v. 214, p. 166-180, 2015. 1387-1811 http://hdl.handle.net/11449/160651 10.1016/j.micromeso.2015.05.007 WOS:000356749900023 WOS000356749900023.pdf |
url |
http://dx.doi.org/10.1016/j.micromeso.2015.05.007 http://hdl.handle.net/11449/160651 |
identifier_str_mv |
Microporous And Mesoporous Materials. Amsterdam: Elsevier Science Bv, v. 214, p. 166-180, 2015. 1387-1811 10.1016/j.micromeso.2015.05.007 WOS:000356749900023 WOS000356749900023.pdf |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Microporous And Mesoporous Materials 1,080 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
166-180 application/pdf |
dc.publisher.none.fl_str_mv |
Elsevier B.V. |
publisher.none.fl_str_mv |
Elsevier B.V. |
dc.source.none.fl_str_mv |
Web of Science reponame:Repositório Institucional da UNESP instname:Universidade Estadual Paulista (UNESP) instacron:UNESP |
instname_str |
Universidade Estadual Paulista (UNESP) |
instacron_str |
UNESP |
institution |
UNESP |
reponame_str |
Repositório Institucional da UNESP |
collection |
Repositório Institucional da UNESP |
repository.name.fl_str_mv |
Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP) |
repository.mail.fl_str_mv |
|
_version_ |
1808129584998121472 |