Surface hidrolysis of polyacrylonitrile with nitrile hydrolysing enzymes from Micrococcus luteus BST20

Detalhes bibliográficos
Autor(a) principal: Fischer-Colbrie, Gudrun
Data de Publicação: 2007
Outros Autores: Matamá, Maria Teresa, Heumann, Sonja, Martinkova, Ludmila, 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/1822/13131
Resumo: A new Micrococcus luteus strain BST20 was isolated with ability to metabolize PAN polymers as sole carbon source. Out of seven synthetized PAN copolymers containing different moieties of acrylic acid and/or vinyl acetate the polymer with lowest crystallinity (PAN with 5% vinyl acetate) was most easily metabolized. 13C labelled PAN was completely converted to the acrylic acid by this strain. M. luteus BST20 produced membrane-bound nitrile hydrolysing enzymes able to convert nitrile groups on PAN powder surface to the corresponding acids. Similarly, nitrile groups on PAN fabrics were transformed to the corresponding acid as indicated by an K/S increased after dying with Methylene blue and the released ammonia. On small soluble substrates the enzyme system showed a preference for aliphatic and aromatic substituted aliphatic nitriles.
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spelling Surface hidrolysis of polyacrylonitrile with nitrile hydrolysing enzymes from Micrococcus luteus BST20Micrococcus luteusNitrilasePolyacrylonitrileSurface modificationA new Micrococcus luteus strain BST20 was isolated with ability to metabolize PAN polymers as sole carbon source. Out of seven synthetized PAN copolymers containing different moieties of acrylic acid and/or vinyl acetate the polymer with lowest crystallinity (PAN with 5% vinyl acetate) was most easily metabolized. 13C labelled PAN was completely converted to the acrylic acid by this strain. M. luteus BST20 produced membrane-bound nitrile hydrolysing enzymes able to convert nitrile groups on PAN powder surface to the corresponding acids. Similarly, nitrile groups on PAN fabrics were transformed to the corresponding acid as indicated by an K/S increased after dying with Methylene blue and the released ammonia. On small soluble substrates the enzyme system showed a preference for aliphatic and aromatic substituted aliphatic nitriles.European Commission - GRD 2000-30110 “Biosyntex”, COSTD25/0002/02ElsevierUniversidade do MinhoFischer-Colbrie, GudrunMatamá, Maria TeresaHeumann, SonjaMartinkova, LudmilaPaulo, Artur CavacoGübitz, Georg M.2007-032007-03-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/1822/13131eng0168-1656http://www.sciencedirect.cominfo: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:RCAAP2023-07-21T12:10:27Zoai:repositorium.sdum.uminho.pt:1822/13131Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T19:02:05.989848Repositório 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 Surface hidrolysis of polyacrylonitrile with nitrile hydrolysing enzymes from Micrococcus luteus BST20
title Surface hidrolysis of polyacrylonitrile with nitrile hydrolysing enzymes from Micrococcus luteus BST20
spellingShingle Surface hidrolysis of polyacrylonitrile with nitrile hydrolysing enzymes from Micrococcus luteus BST20
Fischer-Colbrie, Gudrun
Micrococcus luteus
Nitrilase
Polyacrylonitrile
Surface modification
title_short Surface hidrolysis of polyacrylonitrile with nitrile hydrolysing enzymes from Micrococcus luteus BST20
title_full Surface hidrolysis of polyacrylonitrile with nitrile hydrolysing enzymes from Micrococcus luteus BST20
title_fullStr Surface hidrolysis of polyacrylonitrile with nitrile hydrolysing enzymes from Micrococcus luteus BST20
title_full_unstemmed Surface hidrolysis of polyacrylonitrile with nitrile hydrolysing enzymes from Micrococcus luteus BST20
title_sort Surface hidrolysis of polyacrylonitrile with nitrile hydrolysing enzymes from Micrococcus luteus BST20
author Fischer-Colbrie, Gudrun
author_facet Fischer-Colbrie, Gudrun
Matamá, Maria Teresa
Heumann, Sonja
Martinkova, Ludmila
Paulo, Artur Cavaco
Gübitz, Georg M.
author_role author
author2 Matamá, Maria Teresa
Heumann, Sonja
Martinkova, Ludmila
Paulo, Artur Cavaco
Gübitz, Georg M.
author2_role author
author
author
author
author
dc.contributor.none.fl_str_mv Universidade do Minho
dc.contributor.author.fl_str_mv Fischer-Colbrie, Gudrun
Matamá, Maria Teresa
Heumann, Sonja
Martinkova, Ludmila
Paulo, Artur Cavaco
Gübitz, Georg M.
dc.subject.por.fl_str_mv Micrococcus luteus
Nitrilase
Polyacrylonitrile
Surface modification
topic Micrococcus luteus
Nitrilase
Polyacrylonitrile
Surface modification
description A new Micrococcus luteus strain BST20 was isolated with ability to metabolize PAN polymers as sole carbon source. Out of seven synthetized PAN copolymers containing different moieties of acrylic acid and/or vinyl acetate the polymer with lowest crystallinity (PAN with 5% vinyl acetate) was most easily metabolized. 13C labelled PAN was completely converted to the acrylic acid by this strain. M. luteus BST20 produced membrane-bound nitrile hydrolysing enzymes able to convert nitrile groups on PAN powder surface to the corresponding acids. Similarly, nitrile groups on PAN fabrics were transformed to the corresponding acid as indicated by an K/S increased after dying with Methylene blue and the released ammonia. On small soluble substrates the enzyme system showed a preference for aliphatic and aromatic substituted aliphatic nitriles.
publishDate 2007
dc.date.none.fl_str_mv 2007-03
2007-03-01T00:00:00Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
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status_str publishedVersion
dc.identifier.uri.fl_str_mv http://hdl.handle.net/1822/13131
url http://hdl.handle.net/1822/13131
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 0168-1656
http://www.sciencedirect.com
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dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
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
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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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