Hydrophobic immobilization of Burkholderia cepacia lipase onto octyl-silica for synthesis of flavors esters / Imobilização hidrofóbica da lipase de Burkholderia cepacia sobre octil-sílica para síntese de ésteres de sabores
Autor(a) principal: | |
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Data de Publicação: | 2020 |
Outros Autores: | , , , , , , |
Tipo de documento: | Artigo |
Idioma: | por |
Título da fonte: | Revista Veras |
Texto Completo: | https://ojs.brazilianjournals.com.br/ojs/index.php/BRJD/article/view/9975 |
Resumo: | Burkholderia cepacia lipase (BCL) was immobilized onto silica modified with octyl groups (OS) and the biocatalyst (BCL-OS) was evaluated as its performance in the synthesis in organic medium (synthesis of flavor esters as a model). The maximum support loading was 0.375 genzyme/gsupport, yielding a biocatalyst with an activity of 1197 U/gsupport at pH 7.0 and 50 °C in the hydrolysis of olive oil. The biocatalyst BCL-OS showed to be 9-fold more stable than the free lipase at 60°C in buffer solution (absence of substrates), with an increase of half-life from 16 to 144 h. The physical-chemical characterization of silica, octyl silica, and BCL-OS biocatalyst allowed confirming the immobilization of BCL onto the modified silica. The biocatalyst had an excellent performance in the synthesis of flavor esters, yielding more than 85% esterification yield (based on acid consumption) for acetic and butyric acids as acyl donors, and ethanol, butanol and hexanol as acyl acceptors. The biocatalyst could be recycled by ten 5 h-cycles of butyl butyrate syntheses at 37°C in heptane, retaining around 80% of its initial activity. Therefore, these results indicate that the BCL immobilized onto silica modified with octyl groups is a promising biocatalyst for application in organic syntheses. |
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Hydrophobic immobilization of Burkholderia cepacia lipase onto octyl-silica for synthesis of flavors esters / Imobilização hidrofóbica da lipase de Burkholderia cepacia sobre octil-sílica para síntese de ésteres de saboresoctyl-modified silicahydrophobic immobilizationlipaseesterificationflavor esters.Burkholderia cepacia lipase (BCL) was immobilized onto silica modified with octyl groups (OS) and the biocatalyst (BCL-OS) was evaluated as its performance in the synthesis in organic medium (synthesis of flavor esters as a model). The maximum support loading was 0.375 genzyme/gsupport, yielding a biocatalyst with an activity of 1197 U/gsupport at pH 7.0 and 50 °C in the hydrolysis of olive oil. The biocatalyst BCL-OS showed to be 9-fold more stable than the free lipase at 60°C in buffer solution (absence of substrates), with an increase of half-life from 16 to 144 h. The physical-chemical characterization of silica, octyl silica, and BCL-OS biocatalyst allowed confirming the immobilization of BCL onto the modified silica. The biocatalyst had an excellent performance in the synthesis of flavor esters, yielding more than 85% esterification yield (based on acid consumption) for acetic and butyric acids as acyl donors, and ethanol, butanol and hexanol as acyl acceptors. The biocatalyst could be recycled by ten 5 h-cycles of butyl butyrate syntheses at 37°C in heptane, retaining around 80% of its initial activity. Therefore, these results indicate that the BCL immobilized onto silica modified with octyl groups is a promising biocatalyst for application in organic syntheses. Brazilian Journals Publicações de Periódicos e Editora Ltda.2020-05-13info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfhttps://ojs.brazilianjournals.com.br/ojs/index.php/BRJD/article/view/997510.34117/bjdv6n5-242Brazilian Journal of Development; Vol. 6 No. 5 (2020); 27145-27170Brazilian Journal of Development; Vol. 6 Núm. 5 (2020); 27145-27170Brazilian Journal of Development; v. 6 n. 5 (2020); 27145-271702525-8761reponame:Revista Verasinstname:Instituto Superior de Educação Vera Cruz (VeraCruz)instacron:VERACRUZporhttps://ojs.brazilianjournals.com.br/ojs/index.php/BRJD/article/view/9975/9770Copyright (c) 2020 Brazilian Journal of Developmentinfo:eu-repo/semantics/openAccessBarbosa, Anderson dos SantosSantos, Sara Vitória Gama dosAlmeida, Lays Carvalho deKopp, WillianTardioli, Paulo WaldirGiordano, Raquel de Lima CamargoLima, Álvaro SilvaSoares, Cleide Mara Faria2020-06-16T11:49:32Zoai:ojs2.ojs.brazilianjournals.com.br:article/9975Revistahttp://site.veracruz.edu.br:8087/instituto/revistaveras/index.php/revistaveras/PRIhttp://site.veracruz.edu.br:8087/instituto/revistaveras/index.php/revistaveras/oai||revistaveras@veracruz.edu.br2236-57292236-5729opendoar:2024-10-15T16:06:31.532639Revista Veras - Instituto Superior de Educação Vera Cruz (VeraCruz)false |
dc.title.none.fl_str_mv |
Hydrophobic immobilization of Burkholderia cepacia lipase onto octyl-silica for synthesis of flavors esters / Imobilização hidrofóbica da lipase de Burkholderia cepacia sobre octil-sílica para síntese de ésteres de sabores |
title |
Hydrophobic immobilization of Burkholderia cepacia lipase onto octyl-silica for synthesis of flavors esters / Imobilização hidrofóbica da lipase de Burkholderia cepacia sobre octil-sílica para síntese de ésteres de sabores |
spellingShingle |
Hydrophobic immobilization of Burkholderia cepacia lipase onto octyl-silica for synthesis of flavors esters / Imobilização hidrofóbica da lipase de Burkholderia cepacia sobre octil-sílica para síntese de ésteres de sabores Barbosa, Anderson dos Santos octyl-modified silica hydrophobic immobilization lipase esterification flavor esters. |
title_short |
Hydrophobic immobilization of Burkholderia cepacia lipase onto octyl-silica for synthesis of flavors esters / Imobilização hidrofóbica da lipase de Burkholderia cepacia sobre octil-sílica para síntese de ésteres de sabores |
title_full |
Hydrophobic immobilization of Burkholderia cepacia lipase onto octyl-silica for synthesis of flavors esters / Imobilização hidrofóbica da lipase de Burkholderia cepacia sobre octil-sílica para síntese de ésteres de sabores |
title_fullStr |
Hydrophobic immobilization of Burkholderia cepacia lipase onto octyl-silica for synthesis of flavors esters / Imobilização hidrofóbica da lipase de Burkholderia cepacia sobre octil-sílica para síntese de ésteres de sabores |
title_full_unstemmed |
Hydrophobic immobilization of Burkholderia cepacia lipase onto octyl-silica for synthesis of flavors esters / Imobilização hidrofóbica da lipase de Burkholderia cepacia sobre octil-sílica para síntese de ésteres de sabores |
title_sort |
Hydrophobic immobilization of Burkholderia cepacia lipase onto octyl-silica for synthesis of flavors esters / Imobilização hidrofóbica da lipase de Burkholderia cepacia sobre octil-sílica para síntese de ésteres de sabores |
author |
Barbosa, Anderson dos Santos |
author_facet |
Barbosa, Anderson dos Santos Santos, Sara Vitória Gama dos Almeida, Lays Carvalho de Kopp, Willian Tardioli, Paulo Waldir Giordano, Raquel de Lima Camargo Lima, Álvaro Silva Soares, Cleide Mara Faria |
author_role |
author |
author2 |
Santos, Sara Vitória Gama dos Almeida, Lays Carvalho de Kopp, Willian Tardioli, Paulo Waldir Giordano, Raquel de Lima Camargo Lima, Álvaro Silva Soares, Cleide Mara Faria |
author2_role |
author author author author author author author |
dc.contributor.author.fl_str_mv |
Barbosa, Anderson dos Santos Santos, Sara Vitória Gama dos Almeida, Lays Carvalho de Kopp, Willian Tardioli, Paulo Waldir Giordano, Raquel de Lima Camargo Lima, Álvaro Silva Soares, Cleide Mara Faria |
dc.subject.por.fl_str_mv |
octyl-modified silica hydrophobic immobilization lipase esterification flavor esters. |
topic |
octyl-modified silica hydrophobic immobilization lipase esterification flavor esters. |
description |
Burkholderia cepacia lipase (BCL) was immobilized onto silica modified with octyl groups (OS) and the biocatalyst (BCL-OS) was evaluated as its performance in the synthesis in organic medium (synthesis of flavor esters as a model). The maximum support loading was 0.375 genzyme/gsupport, yielding a biocatalyst with an activity of 1197 U/gsupport at pH 7.0 and 50 °C in the hydrolysis of olive oil. The biocatalyst BCL-OS showed to be 9-fold more stable than the free lipase at 60°C in buffer solution (absence of substrates), with an increase of half-life from 16 to 144 h. The physical-chemical characterization of silica, octyl silica, and BCL-OS biocatalyst allowed confirming the immobilization of BCL onto the modified silica. The biocatalyst had an excellent performance in the synthesis of flavor esters, yielding more than 85% esterification yield (based on acid consumption) for acetic and butyric acids as acyl donors, and ethanol, butanol and hexanol as acyl acceptors. The biocatalyst could be recycled by ten 5 h-cycles of butyl butyrate syntheses at 37°C in heptane, retaining around 80% of its initial activity. Therefore, these results indicate that the BCL immobilized onto silica modified with octyl groups is a promising biocatalyst for application in organic syntheses. |
publishDate |
2020 |
dc.date.none.fl_str_mv |
2020-05-13 |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
https://ojs.brazilianjournals.com.br/ojs/index.php/BRJD/article/view/9975 10.34117/bjdv6n5-242 |
url |
https://ojs.brazilianjournals.com.br/ojs/index.php/BRJD/article/view/9975 |
identifier_str_mv |
10.34117/bjdv6n5-242 |
dc.language.iso.fl_str_mv |
por |
language |
por |
dc.relation.none.fl_str_mv |
https://ojs.brazilianjournals.com.br/ojs/index.php/BRJD/article/view/9975/9770 |
dc.rights.driver.fl_str_mv |
Copyright (c) 2020 Brazilian Journal of Development info:eu-repo/semantics/openAccess |
rights_invalid_str_mv |
Copyright (c) 2020 Brazilian Journal of Development |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
application/pdf |
dc.publisher.none.fl_str_mv |
Brazilian Journals Publicações de Periódicos e Editora Ltda. |
publisher.none.fl_str_mv |
Brazilian Journals Publicações de Periódicos e Editora Ltda. |
dc.source.none.fl_str_mv |
Brazilian Journal of Development; Vol. 6 No. 5 (2020); 27145-27170 Brazilian Journal of Development; Vol. 6 Núm. 5 (2020); 27145-27170 Brazilian Journal of Development; v. 6 n. 5 (2020); 27145-27170 2525-8761 reponame:Revista Veras instname:Instituto Superior de Educação Vera Cruz (VeraCruz) instacron:VERACRUZ |
instname_str |
Instituto Superior de Educação Vera Cruz (VeraCruz) |
instacron_str |
VERACRUZ |
institution |
VERACRUZ |
reponame_str |
Revista Veras |
collection |
Revista Veras |
repository.name.fl_str_mv |
Revista Veras - Instituto Superior de Educação Vera Cruz (VeraCruz) |
repository.mail.fl_str_mv |
||revistaveras@veracruz.edu.br |
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1813645451515133952 |