Exploring metagenomic enzymes: A novel esterase useful for short-chain ester synthesis
Autor(a) principal: | |
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Data de Publicação: | 2020 |
Outros Autores: | , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNESP |
Texto Completo: | http://dx.doi.org/10.3390/catal10101100 http://hdl.handle.net/11449/205229 |
Resumo: | Enzyme-mediated esterification reactions can be a promising alternative to produce esters of commercial interest, replacing conventional chemical processes. The aim of this work was to verify the potential of an esterase for ester synthesis. For that, recombinant lipolytic enzyme EST5 was purified and presented higher activity at pH 7.5, 45◦ C, with a Tm of 47◦ C. Also, the enzyme remained at least 50% active at low temperatures and exhibited broad substrate specificity toward p-nitrophenol esters with highest activity for p-nitrophenyl valerate with a Kcat /Km of 1533 s−1 mM−1. This esterase exerted great properties that make it useful for industrial applications, since EST5 remained stable in the presence of up to 10% methanol and 20% dimethyl sulfoxide. Also, preliminary studies in esterification reactions for the synthesis of methyl butyrate led to a specific activity of 127.04 U·mg−1. The enzyme showed higher esterification activity compared to other literature results, including commercial enzymes such as LIP4 and CL of Candida rugosa assayed with butyric acid and propanol which showed esterification activity of 86.5 and 15.83 U·mg−1, respectively. In conclusion, EST5 has potential for synthesis of flavor esters, providing a concept for its application in biotechnological processes. |
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Exploring metagenomic enzymes: A novel esterase useful for short-chain ester synthesisEsterificationFamily VFlavor estersLipolytic enzymesMetagenomeEnzyme-mediated esterification reactions can be a promising alternative to produce esters of commercial interest, replacing conventional chemical processes. The aim of this work was to verify the potential of an esterase for ester synthesis. For that, recombinant lipolytic enzyme EST5 was purified and presented higher activity at pH 7.5, 45◦ C, with a Tm of 47◦ C. Also, the enzyme remained at least 50% active at low temperatures and exhibited broad substrate specificity toward p-nitrophenol esters with highest activity for p-nitrophenyl valerate with a Kcat /Km of 1533 s−1 mM−1. This esterase exerted great properties that make it useful for industrial applications, since EST5 remained stable in the presence of up to 10% methanol and 20% dimethyl sulfoxide. Also, preliminary studies in esterification reactions for the synthesis of methyl butyrate led to a specific activity of 127.04 U·mg−1. The enzyme showed higher esterification activity compared to other literature results, including commercial enzymes such as LIP4 and CL of Candida rugosa assayed with butyric acid and propanol which showed esterification activity of 86.5 and 15.83 U·mg−1, respectively. In conclusion, EST5 has potential for synthesis of flavor esters, providing a concept for its application in biotechnological processes.Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Department of Technology São Paulo State University (UNESP)Institute of Biomedical Sciences (ICB III) University of São Paulo (USP)Institute of Biosciences Languages and Exact Sciences Department of Chemistry and Environmental Sciences São Paulo State University (UNESP)Department of Technology São Paulo State University (UNESP)Institute of Biosciences Languages and Exact Sciences Department of Chemistry and Environmental Sciences São Paulo State University (UNESP)FAPESP: 2011/09064-6FAPESP: 2013/03568-8Universidade Estadual Paulista (Unesp)Universidade de São Paulo (USP)Maester, Thaís Carvalho [UNESP]Pereira, Mariana Rangel [UNESP]Gibertoni Malaman, Aliandra M. [UNESP]Borges, Janaina Pires [UNESP]Pereira, Pâmela Aparecida Maldaner [UNESP]Lemos, Eliana G. M. [UNESP]2021-06-25T10:11:59Z2021-06-25T10:11:59Z2020-10-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article1-18http://dx.doi.org/10.3390/catal10101100Catalysts, v. 10, n. 10, p. 1-18, 2020.2073-4344http://hdl.handle.net/11449/20522910.3390/catal101011002-s2.0-85091678109Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengCatalystsinfo:eu-repo/semantics/openAccess2021-10-23T12:19:08Zoai:repositorio.unesp.br:11449/205229Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T17:08:44.893474Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
dc.title.none.fl_str_mv |
Exploring metagenomic enzymes: A novel esterase useful for short-chain ester synthesis |
title |
Exploring metagenomic enzymes: A novel esterase useful for short-chain ester synthesis |
spellingShingle |
Exploring metagenomic enzymes: A novel esterase useful for short-chain ester synthesis Maester, Thaís Carvalho [UNESP] Esterification Family V Flavor esters Lipolytic enzymes Metagenome |
title_short |
Exploring metagenomic enzymes: A novel esterase useful for short-chain ester synthesis |
title_full |
Exploring metagenomic enzymes: A novel esterase useful for short-chain ester synthesis |
title_fullStr |
Exploring metagenomic enzymes: A novel esterase useful for short-chain ester synthesis |
title_full_unstemmed |
Exploring metagenomic enzymes: A novel esterase useful for short-chain ester synthesis |
title_sort |
Exploring metagenomic enzymes: A novel esterase useful for short-chain ester synthesis |
author |
Maester, Thaís Carvalho [UNESP] |
author_facet |
Maester, Thaís Carvalho [UNESP] Pereira, Mariana Rangel [UNESP] Gibertoni Malaman, Aliandra M. [UNESP] Borges, Janaina Pires [UNESP] Pereira, Pâmela Aparecida Maldaner [UNESP] Lemos, Eliana G. M. [UNESP] |
author_role |
author |
author2 |
Pereira, Mariana Rangel [UNESP] Gibertoni Malaman, Aliandra M. [UNESP] Borges, Janaina Pires [UNESP] Pereira, Pâmela Aparecida Maldaner [UNESP] Lemos, Eliana G. M. [UNESP] |
author2_role |
author author author author author |
dc.contributor.none.fl_str_mv |
Universidade Estadual Paulista (Unesp) Universidade de São Paulo (USP) |
dc.contributor.author.fl_str_mv |
Maester, Thaís Carvalho [UNESP] Pereira, Mariana Rangel [UNESP] Gibertoni Malaman, Aliandra M. [UNESP] Borges, Janaina Pires [UNESP] Pereira, Pâmela Aparecida Maldaner [UNESP] Lemos, Eliana G. M. [UNESP] |
dc.subject.por.fl_str_mv |
Esterification Family V Flavor esters Lipolytic enzymes Metagenome |
topic |
Esterification Family V Flavor esters Lipolytic enzymes Metagenome |
description |
Enzyme-mediated esterification reactions can be a promising alternative to produce esters of commercial interest, replacing conventional chemical processes. The aim of this work was to verify the potential of an esterase for ester synthesis. For that, recombinant lipolytic enzyme EST5 was purified and presented higher activity at pH 7.5, 45◦ C, with a Tm of 47◦ C. Also, the enzyme remained at least 50% active at low temperatures and exhibited broad substrate specificity toward p-nitrophenol esters with highest activity for p-nitrophenyl valerate with a Kcat /Km of 1533 s−1 mM−1. This esterase exerted great properties that make it useful for industrial applications, since EST5 remained stable in the presence of up to 10% methanol and 20% dimethyl sulfoxide. Also, preliminary studies in esterification reactions for the synthesis of methyl butyrate led to a specific activity of 127.04 U·mg−1. The enzyme showed higher esterification activity compared to other literature results, including commercial enzymes such as LIP4 and CL of Candida rugosa assayed with butyric acid and propanol which showed esterification activity of 86.5 and 15.83 U·mg−1, respectively. In conclusion, EST5 has potential for synthesis of flavor esters, providing a concept for its application in biotechnological processes. |
publishDate |
2020 |
dc.date.none.fl_str_mv |
2020-10-01 2021-06-25T10:11:59Z 2021-06-25T10:11:59Z |
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/10.3390/catal10101100 Catalysts, v. 10, n. 10, p. 1-18, 2020. 2073-4344 http://hdl.handle.net/11449/205229 10.3390/catal10101100 2-s2.0-85091678109 |
url |
http://dx.doi.org/10.3390/catal10101100 http://hdl.handle.net/11449/205229 |
identifier_str_mv |
Catalysts, v. 10, n. 10, p. 1-18, 2020. 2073-4344 10.3390/catal10101100 2-s2.0-85091678109 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Catalysts |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
1-18 |
dc.source.none.fl_str_mv |
Scopus 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_ |
1808128760888688640 |