A novel aryl acylamidase from Nocardia farcinica hydrolyses polyamide

Detalhes bibliográficos
Autor(a) principal: Heumann, Sonja
Data de Publicação: 2009
Outros Autores: Eberl, A., Fischer-Colbrie, Gudrun, Pobeheim, Herbert, Kaufmann, F., Ribitsch, D., Paulo, Artur Cavaco, Gübitz, Georg M.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/1822/17322
Resumo: An alkali stable polyamidase was isolated from a new strain of Nocardia farcinica. The enzyme consists of four subunits with a total molecular weight of 190 kDa. The polyamidase cleaved amide and ester bonds of water insoluble model substrates like adipic acid bishexylamide and bis(benzoyloxyethyl)terephthalate and hydrolyzed different soluble amides to the corresponding acid. Treatment of polyamide 6 with this amidase led to an increased hydrophilicity based on rising height and tensiometry measurements and evidence of surface hydrolysis of polyamide 6 is shown. In addition to amidase activity, the enzyme showed activity on p-nitrophenylbutyrate. On hexanoamide the amidase exhibited a Km value of 5.5 mM compared to 0.07 mM for p-nitroacetanilide. The polyamidase belongs to the amidase signature family and is closely related to aryl acylamidases from different strains/species of Nocardia and to the 6-aminohexanoate-cyclic dimer hydrolase (EI) from Arthrobacter sp. KI72.
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spelling A novel aryl acylamidase from Nocardia farcinica hydrolyses polyamidePolyamideAmidaseNocardiaScience & TechnologyAn alkali stable polyamidase was isolated from a new strain of Nocardia farcinica. The enzyme consists of four subunits with a total molecular weight of 190 kDa. The polyamidase cleaved amide and ester bonds of water insoluble model substrates like adipic acid bishexylamide and bis(benzoyloxyethyl)terephthalate and hydrolyzed different soluble amides to the corresponding acid. Treatment of polyamide 6 with this amidase led to an increased hydrophilicity based on rising height and tensiometry measurements and evidence of surface hydrolysis of polyamide 6 is shown. In addition to amidase activity, the enzyme showed activity on p-nitrophenylbutyrate. On hexanoamide the amidase exhibited a Km value of 5.5 mM compared to 0.07 mM for p-nitroacetanilide. The polyamidase belongs to the amidase signature family and is closely related to aryl acylamidases from different strains/species of Nocardia and to the 6-aminohexanoate-cyclic dimer hydrolase (EI) from Arthrobacter sp. KI72.We would like to thank Markus List for measuring of the hydrophilicity of PA fabrics. The research was financed by the Commission of the European Union (GRD2000-30110 BIOSNYTEX), the Austrian FFG, the SFG, the City of Graz, and the Province of Styria.WileyUniversidade do MinhoHeumann, SonjaEberl, A.Fischer-Colbrie, GudrunPobeheim, HerbertKaufmann, F.Ribitsch, D.Paulo, Artur CavacoGübitz, Georg M.2009-112009-11-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/1822/17322eng1097-029010.1002/bit.2213918942140info:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2023-07-21T12:40:48Zoai:repositorium.sdum.uminho.pt:1822/17322Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T19:37:39.970105Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse
dc.title.none.fl_str_mv A novel aryl acylamidase from Nocardia farcinica hydrolyses polyamide
title A novel aryl acylamidase from Nocardia farcinica hydrolyses polyamide
spellingShingle A novel aryl acylamidase from Nocardia farcinica hydrolyses polyamide
Heumann, Sonja
Polyamide
Amidase
Nocardia
Science & Technology
title_short A novel aryl acylamidase from Nocardia farcinica hydrolyses polyamide
title_full A novel aryl acylamidase from Nocardia farcinica hydrolyses polyamide
title_fullStr A novel aryl acylamidase from Nocardia farcinica hydrolyses polyamide
title_full_unstemmed A novel aryl acylamidase from Nocardia farcinica hydrolyses polyamide
title_sort A novel aryl acylamidase from Nocardia farcinica hydrolyses polyamide
author Heumann, Sonja
author_facet Heumann, Sonja
Eberl, A.
Fischer-Colbrie, Gudrun
Pobeheim, Herbert
Kaufmann, F.
Ribitsch, D.
Paulo, Artur Cavaco
Gübitz, Georg M.
author_role author
author2 Eberl, A.
Fischer-Colbrie, Gudrun
Pobeheim, Herbert
Kaufmann, F.
Ribitsch, D.
Paulo, Artur Cavaco
Gübitz, Georg M.
author2_role author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Universidade do Minho
dc.contributor.author.fl_str_mv Heumann, Sonja
Eberl, A.
Fischer-Colbrie, Gudrun
Pobeheim, Herbert
Kaufmann, F.
Ribitsch, D.
Paulo, Artur Cavaco
Gübitz, Georg M.
dc.subject.por.fl_str_mv Polyamide
Amidase
Nocardia
Science & Technology
topic Polyamide
Amidase
Nocardia
Science & Technology
description An alkali stable polyamidase was isolated from a new strain of Nocardia farcinica. The enzyme consists of four subunits with a total molecular weight of 190 kDa. The polyamidase cleaved amide and ester bonds of water insoluble model substrates like adipic acid bishexylamide and bis(benzoyloxyethyl)terephthalate and hydrolyzed different soluble amides to the corresponding acid. Treatment of polyamide 6 with this amidase led to an increased hydrophilicity based on rising height and tensiometry measurements and evidence of surface hydrolysis of polyamide 6 is shown. In addition to amidase activity, the enzyme showed activity on p-nitrophenylbutyrate. On hexanoamide the amidase exhibited a Km value of 5.5 mM compared to 0.07 mM for p-nitroacetanilide. The polyamidase belongs to the amidase signature family and is closely related to aryl acylamidases from different strains/species of Nocardia and to the 6-aminohexanoate-cyclic dimer hydrolase (EI) from Arthrobacter sp. KI72.
publishDate 2009
dc.date.none.fl_str_mv 2009-11
2009-11-01T00:00:00Z
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://hdl.handle.net/1822/17322
url http://hdl.handle.net/1822/17322
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 1097-0290
10.1002/bit.22139
18942140
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Wiley
publisher.none.fl_str_mv Wiley
dc.source.none.fl_str_mv reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron:RCAAP
instname_str Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron_str RCAAP
institution RCAAP
reponame_str Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
collection Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
repository.name.fl_str_mv Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
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