Surface hydrolysis of polyamide with a new polyamidase from Beauveria brongniartii
Main Author: | |
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Publication Date: | 2008 |
Other Authors: | , , , , |
Format: | Article |
Language: | eng |
Source: | Repositórios Científicos de Acesso Aberto de Portugal (RCAAP) |
Download full: | http://hdl.handle.net/1822/17287 |
Summary: | 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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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:Repositórios Científicos de Acesso Aberto de Portugal (RCAAP)instname:FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologiainstacron:RCAAP2024-05-11T07:01:07Zoai:repositorium.sdum.uminho.pt:1822/17287Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireinfo@rcaap.ptopendoar:https://opendoar.ac.uk/repository/71602025-05-28T16:12:30.035157Repositórios Científicos de Acesso Aberto de Portugal (RCAAP) - FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologiafalse |
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 |
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Repositórios Científicos de Acesso Aberto de Portugal (RCAAP) |
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