Surface hydrolysis of polyamide with a new polyamidase from Beauveria brongniartii

Detalhes bibliográficos
Autor(a) principal: Almansa, Eva
Data de Publicação: 2008
Outros Autores: Heumann, Sonja, Eberl, A., Kaufmann, F., 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/1822/17287
Resumo: Twelve fungi were screened for the potential of their extracellular enzymes to increase the hydrophilicity of polyamide (PA) materials. The most pronounced increase in hydrophilicity was found for enzymes from Beauveria brongniartii and B. bassiana. The 55 kDa polyamidase from B. brongniartii was purified using ultrafiltration, anion exchange chromatography and size exclusion chromatography. This polyamidase was able to hydrolyse adipic acid bishexylamide and various typical amidase substrates, but did not show protease activity. In contrast, the 27 kDa protease from B. brongniartii did not show activity on PA. The improvement of hydrophilicity due to hydrolysis with the 55 kDa polyamidase from B. brongniartii based on rising height was 11 cm for PA 6 Perlon fibres and 5 cm for PA 6.6 Nylon. The drop dissipation measurement corroborated the improvement of the hydrophilicity giving 7 s and less than 1 s for the two enzyme treated materials, respectively. The surface tension s of Perlon increased from 46.1 to 67.4 mNm after enzyme treatment.
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spelling Surface hydrolysis of polyamide with a new polyamidase from Beauveria brongniartiiBeauveria brongniartiiRising heightPolyamide fibresPolyamidaseScience & TechnologyTwelve fungi were screened for the potential of their extracellular enzymes to increase the hydrophilicity of polyamide (PA) materials. The most pronounced increase in hydrophilicity was found for enzymes from Beauveria brongniartii and B. bassiana. The 55 kDa polyamidase from B. brongniartii was purified using ultrafiltration, anion exchange chromatography and size exclusion chromatography. This polyamidase was able to hydrolyse adipic acid bishexylamide and various typical amidase substrates, but did not show protease activity. In contrast, the 27 kDa protease from B. brongniartii did not show activity on PA. The improvement of hydrophilicity due to hydrolysis with the 55 kDa polyamidase from B. brongniartii based on rising height was 11 cm for PA 6 Perlon fibres and 5 cm for PA 6.6 Nylon. The drop dissipation measurement corroborated the improvement of the hydrophilicity giving 7 s and less than 1 s for the two enzyme treated materials, respectively. The surface tension s of Perlon increased from 46.1 to 67.4 mNm after enzyme treatment.The research was financed by the SFG, the FFG, the city of Graz and the province of Styria and by European Commission within the project GRD 2000-30110 BiosyntexInforma HealthcareUniversidade do MinhoAlmansa, EvaHeumann, SonjaEberl, A.Kaufmann, F.Paulo, Artur CavacoGübitz, Georg M.20082008-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/1822/17287eng1024-242210.1080/10242420802323433http://informahealthcare.com/doi/abs/10.1080/10242420802323433info: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:RCAAP2023-07-21T12:43:25Zoai:repositorium.sdum.uminho.pt:1822/17287Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T19:40:54.066391Repositório 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 hydrolysis of polyamide with a new polyamidase from Beauveria brongniartii
title Surface hydrolysis of polyamide with a new polyamidase from Beauveria brongniartii
spellingShingle Surface hydrolysis of polyamide with a new polyamidase from Beauveria brongniartii
Almansa, Eva
Beauveria brongniartii
Rising height
Polyamide fibres
Polyamidase
Science & Technology
title_short Surface hydrolysis of polyamide with a new polyamidase from Beauveria brongniartii
title_full Surface hydrolysis of polyamide with a new polyamidase from Beauveria brongniartii
title_fullStr Surface hydrolysis of polyamide with a new polyamidase from Beauveria brongniartii
title_full_unstemmed Surface hydrolysis of polyamide with a new polyamidase from Beauveria brongniartii
title_sort Surface hydrolysis of polyamide with a new polyamidase from Beauveria brongniartii
author Almansa, Eva
author_facet Almansa, Eva
Heumann, Sonja
Eberl, A.
Kaufmann, F.
Paulo, Artur Cavaco
Gübitz, Georg M.
author_role author
author2 Heumann, Sonja
Eberl, A.
Kaufmann, F.
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 Almansa, Eva
Heumann, Sonja
Eberl, A.
Kaufmann, F.
Paulo, Artur Cavaco
Gübitz, Georg M.
dc.subject.por.fl_str_mv Beauveria brongniartii
Rising height
Polyamide fibres
Polyamidase
Science & Technology
topic Beauveria brongniartii
Rising height
Polyamide fibres
Polyamidase
Science & Technology
description Twelve fungi were screened for the potential of their extracellular enzymes to increase the hydrophilicity of polyamide (PA) materials. The most pronounced increase in hydrophilicity was found for enzymes from Beauveria brongniartii and B. bassiana. The 55 kDa polyamidase from B. brongniartii was purified using ultrafiltration, anion exchange chromatography and size exclusion chromatography. This polyamidase was able to hydrolyse adipic acid bishexylamide and various typical amidase substrates, but did not show protease activity. In contrast, the 27 kDa protease from B. brongniartii did not show activity on PA. The improvement of hydrophilicity due to hydrolysis with the 55 kDa polyamidase from B. brongniartii based on rising height was 11 cm for PA 6 Perlon fibres and 5 cm for PA 6.6 Nylon. The drop dissipation measurement corroborated the improvement of the hydrophilicity giving 7 s and less than 1 s for the two enzyme treated materials, respectively. The surface tension s of Perlon increased from 46.1 to 67.4 mNm after enzyme treatment.
publishDate 2008
dc.date.none.fl_str_mv 2008
2008-01-01T00:00:00Z
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/1822/17287
url http://hdl.handle.net/1822/17287
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 1024-2422
10.1080/10242420802323433
http://informahealthcare.com/doi/abs/10.1080/10242420802323433
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 Informa Healthcare
publisher.none.fl_str_mv Informa Healthcare
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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