Biotransformations of nitriles mediated by in vivo nitrile hydratase of Rhodococcus erythropolis ATCC 4277 heterologously expressed in E. Coli

Detalhes bibliográficos
Autor(a) principal: Moraes, Maraylla I. [UNESP]
Data de Publicação: 2023
Outros Autores: Iglesias, César, Teixeira, Iris S. [UNESP], Milagre, Humberto M.S. [UNESP], Giordano, Sonia Rodríguez, Milagre, Cintia D.F. [UNESP]
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UNESP
Texto Completo: http://dx.doi.org/10.1016/j.rechem.2022.100760
http://hdl.handle.net/11449/246628
Resumo: Nitrile hydratase activity has been reported as an exciting alternative for the industrial production of a variety of compounds overwhelming its chemical counterpart; despite this, until now, a few enzymes have been thoroughly studied. Efficient expression of nitrile hydratase enzymes has been the bottleneck to explore this activity. Here, we report the cloning and expression of Rhodococcus erythropolis ATCC 4277 nitrile hydratase (α- and β-subunits) and the correspondent activator gene. Furthermore, substrate scope with whole cells of recombinant E. coli demonstrates that this Fe-type NHase could hydrate a wide range of aliphatic and aromatic nitrile with high conversion rates and moderate enantiomeric excess.
id UNSP_2b1e6ac166dd28596d14bbce9693fe81
oai_identifier_str oai:repositorio.unesp.br:11449/246628
network_acronym_str UNSP
network_name_str Repositório Institucional da UNESP
repository_id_str 2946
spelling Biotransformations of nitriles mediated by in vivo nitrile hydratase of Rhodococcus erythropolis ATCC 4277 heterologously expressed in E. ColiAmidesBiocatalysisNitrile hydrataseNitrilesRestriction free cloningNitrile hydratase activity has been reported as an exciting alternative for the industrial production of a variety of compounds overwhelming its chemical counterpart; despite this, until now, a few enzymes have been thoroughly studied. Efficient expression of nitrile hydratase enzymes has been the bottleneck to explore this activity. Here, we report the cloning and expression of Rhodococcus erythropolis ATCC 4277 nitrile hydratase (α- and β-subunits) and the correspondent activator gene. Furthermore, substrate scope with whole cells of recombinant E. coli demonstrates that this Fe-type NHase could hydrate a wide range of aliphatic and aromatic nitrile with high conversion rates and moderate enantiomeric excess.Institute of Chemistry UNESP – São Paulo State University, São PauloArea Microbiología DEPBIO Facultad de Química Universidad de la República, Gral. Flores 2124Institute of Chemistry UNESP – São Paulo State University, São PauloUniversidade Estadual Paulista (UNESP)Universidad de la RepúblicaMoraes, Maraylla I. [UNESP]Iglesias, CésarTeixeira, Iris S. [UNESP]Milagre, Humberto M.S. [UNESP]Giordano, Sonia RodríguezMilagre, Cintia D.F. [UNESP]2023-07-29T12:46:05Z2023-07-29T12:46:05Z2023-01-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlehttp://dx.doi.org/10.1016/j.rechem.2022.100760Results in Chemistry, v. 5.2211-7156http://hdl.handle.net/11449/24662810.1016/j.rechem.2022.1007602-s2.0-85146022209Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengResults in Chemistryinfo:eu-repo/semantics/openAccess2023-07-29T12:46:05Zoai:repositorio.unesp.br:11449/246628Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T14:09:14.882334Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false
dc.title.none.fl_str_mv Biotransformations of nitriles mediated by in vivo nitrile hydratase of Rhodococcus erythropolis ATCC 4277 heterologously expressed in E. Coli
title Biotransformations of nitriles mediated by in vivo nitrile hydratase of Rhodococcus erythropolis ATCC 4277 heterologously expressed in E. Coli
spellingShingle Biotransformations of nitriles mediated by in vivo nitrile hydratase of Rhodococcus erythropolis ATCC 4277 heterologously expressed in E. Coli
Moraes, Maraylla I. [UNESP]
Amides
Biocatalysis
Nitrile hydratase
Nitriles
Restriction free cloning
title_short Biotransformations of nitriles mediated by in vivo nitrile hydratase of Rhodococcus erythropolis ATCC 4277 heterologously expressed in E. Coli
title_full Biotransformations of nitriles mediated by in vivo nitrile hydratase of Rhodococcus erythropolis ATCC 4277 heterologously expressed in E. Coli
title_fullStr Biotransformations of nitriles mediated by in vivo nitrile hydratase of Rhodococcus erythropolis ATCC 4277 heterologously expressed in E. Coli
title_full_unstemmed Biotransformations of nitriles mediated by in vivo nitrile hydratase of Rhodococcus erythropolis ATCC 4277 heterologously expressed in E. Coli
title_sort Biotransformations of nitriles mediated by in vivo nitrile hydratase of Rhodococcus erythropolis ATCC 4277 heterologously expressed in E. Coli
author Moraes, Maraylla I. [UNESP]
author_facet Moraes, Maraylla I. [UNESP]
Iglesias, César
Teixeira, Iris S. [UNESP]
Milagre, Humberto M.S. [UNESP]
Giordano, Sonia Rodríguez
Milagre, Cintia D.F. [UNESP]
author_role author
author2 Iglesias, César
Teixeira, Iris S. [UNESP]
Milagre, Humberto M.S. [UNESP]
Giordano, Sonia Rodríguez
Milagre, Cintia D.F. [UNESP]
author2_role author
author
author
author
author
dc.contributor.none.fl_str_mv Universidade Estadual Paulista (UNESP)
Universidad de la República
dc.contributor.author.fl_str_mv Moraes, Maraylla I. [UNESP]
Iglesias, César
Teixeira, Iris S. [UNESP]
Milagre, Humberto M.S. [UNESP]
Giordano, Sonia Rodríguez
Milagre, Cintia D.F. [UNESP]
dc.subject.por.fl_str_mv Amides
Biocatalysis
Nitrile hydratase
Nitriles
Restriction free cloning
topic Amides
Biocatalysis
Nitrile hydratase
Nitriles
Restriction free cloning
description Nitrile hydratase activity has been reported as an exciting alternative for the industrial production of a variety of compounds overwhelming its chemical counterpart; despite this, until now, a few enzymes have been thoroughly studied. Efficient expression of nitrile hydratase enzymes has been the bottleneck to explore this activity. Here, we report the cloning and expression of Rhodococcus erythropolis ATCC 4277 nitrile hydratase (α- and β-subunits) and the correspondent activator gene. Furthermore, substrate scope with whole cells of recombinant E. coli demonstrates that this Fe-type NHase could hydrate a wide range of aliphatic and aromatic nitrile with high conversion rates and moderate enantiomeric excess.
publishDate 2023
dc.date.none.fl_str_mv 2023-07-29T12:46:05Z
2023-07-29T12:46:05Z
2023-01-01
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.rechem.2022.100760
Results in Chemistry, v. 5.
2211-7156
http://hdl.handle.net/11449/246628
10.1016/j.rechem.2022.100760
2-s2.0-85146022209
url http://dx.doi.org/10.1016/j.rechem.2022.100760
http://hdl.handle.net/11449/246628
identifier_str_mv Results in Chemistry, v. 5.
2211-7156
10.1016/j.rechem.2022.100760
2-s2.0-85146022209
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Results in Chemistry
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
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_ 1808128323069411328

Registros relacionados