Surface hidrolysis of polyacrylonitrile with nitrile hydrolysing enzymes from Micrococcus luteus BST20
Autor(a) principal: | |
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Data de Publicação: | 2007 |
Outros Autores: | , , , , |
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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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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7160 |
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 |
format |
article |
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 |
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 |
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 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 |
repository.mail.fl_str_mv |
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1799132421452464128 |