Lipases efficiently stearate and cutinases acetylate the surface of arabinoxylan films

Detalhes bibliográficos
Autor(a) principal: Stepan, A. M.
Data de Publicação: 2013
Outros Autores: Anasontzis, G. E., Matamá, Maria Teresa, Paulo, Artur Cavaco, Olsson, L., Gatenholm, P.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/1822/25519
Resumo: This is the first report on successful enzyme catalyzed surface esterification of hemicellulose films. Enzyme catalyzed surface acetylation with vinyl acetate and stearation with vinyl stearate were studied on rye arabinoxylan (AX) films. Different surface analytical techniques (FT-IR, TOF-SIMS, ESCA, CA) show that lipases from Mucor javanicus, Rhizopus oryzae and Candida rugosa successfully surface stearate AX films and that a cutinase from Fusarium solani pisi surface acetylates these films. The specificities of cutinase and lipases were also compared, and higher activity was observed for lipases utilizing long alkyl chain substrates while higher activity was observed for cutinase utilizing shorter alkyl chain substrates. The contact angle analysis showed films with increased initial hydrophobicity on the surfaces.
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spelling Lipases efficiently stearate and cutinases acetylate the surface of arabinoxylan filmsHemicelluloseArabinoxylanFilmSurface esterificationEnzymatic modificationScience & TechnologyThis is the first report on successful enzyme catalyzed surface esterification of hemicellulose films. Enzyme catalyzed surface acetylation with vinyl acetate and stearation with vinyl stearate were studied on rye arabinoxylan (AX) films. Different surface analytical techniques (FT-IR, TOF-SIMS, ESCA, CA) show that lipases from Mucor javanicus, Rhizopus oryzae and Candida rugosa successfully surface stearate AX films and that a cutinase from Fusarium solani pisi surface acetylates these films. The specificities of cutinase and lipases were also compared, and higher activity was observed for lipases utilizing long alkyl chain substrates while higher activity was observed for cutinase utilizing shorter alkyl chain substrates. The contact angle analysis showed films with increased initial hydrophobicity on the surfaces.Anne Wendel, Anders Martensson and Per Malmberg from Chalmers University of Technology are acknowledged for their help in the ESCA, FT-IR and SIMS measurements. The Knut and Alice Wallenberg Foundation is gratefully acknowledged for donating a base for a Swedish Research Center, the Wallenberg Wood Science Center, thus financing this work.ElsevierElsevier BVUniversidade do MinhoStepan, A. M.Anasontzis, G. E.Matamá, Maria TeresaPaulo, Artur CavacoOlsson, L.Gatenholm, P.20132013-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/1822/25519eng0168-16560168-165610.1016/j.jbiotec.2013.06.00423774036www.elsevier.com/locate/jbiotecinfo: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:RCAAP2023-07-21T12:54:15Zoai:repositorium.sdum.uminho.pt:1822/25519Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T19:53:48.089001Repositório 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 Lipases efficiently stearate and cutinases acetylate the surface of arabinoxylan films
title Lipases efficiently stearate and cutinases acetylate the surface of arabinoxylan films
spellingShingle Lipases efficiently stearate and cutinases acetylate the surface of arabinoxylan films
Stepan, A. M.
Hemicellulose
Arabinoxylan
Film
Surface esterification
Enzymatic modification
Science & Technology
title_short Lipases efficiently stearate and cutinases acetylate the surface of arabinoxylan films
title_full Lipases efficiently stearate and cutinases acetylate the surface of arabinoxylan films
title_fullStr Lipases efficiently stearate and cutinases acetylate the surface of arabinoxylan films
title_full_unstemmed Lipases efficiently stearate and cutinases acetylate the surface of arabinoxylan films
title_sort Lipases efficiently stearate and cutinases acetylate the surface of arabinoxylan films
author Stepan, A. M.
author_facet Stepan, A. M.
Anasontzis, G. E.
Matamá, Maria Teresa
Paulo, Artur Cavaco
Olsson, L.
Gatenholm, P.
author_role author
author2 Anasontzis, G. E.
Matamá, Maria Teresa
Paulo, Artur Cavaco
Olsson, L.
Gatenholm, P.
author2_role author
author
author
author
author
dc.contributor.none.fl_str_mv Universidade do Minho
dc.contributor.author.fl_str_mv Stepan, A. M.
Anasontzis, G. E.
Matamá, Maria Teresa
Paulo, Artur Cavaco
Olsson, L.
Gatenholm, P.
dc.subject.por.fl_str_mv Hemicellulose
Arabinoxylan
Film
Surface esterification
Enzymatic modification
Science & Technology
topic Hemicellulose
Arabinoxylan
Film
Surface esterification
Enzymatic modification
Science & Technology
description This is the first report on successful enzyme catalyzed surface esterification of hemicellulose films. Enzyme catalyzed surface acetylation with vinyl acetate and stearation with vinyl stearate were studied on rye arabinoxylan (AX) films. Different surface analytical techniques (FT-IR, TOF-SIMS, ESCA, CA) show that lipases from Mucor javanicus, Rhizopus oryzae and Candida rugosa successfully surface stearate AX films and that a cutinase from Fusarium solani pisi surface acetylates these films. The specificities of cutinase and lipases were also compared, and higher activity was observed for lipases utilizing long alkyl chain substrates while higher activity was observed for cutinase utilizing shorter alkyl chain substrates. The contact angle analysis showed films with increased initial hydrophobicity on the surfaces.
publishDate 2013
dc.date.none.fl_str_mv 2013
2013-01-01T00:00:00Z
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/1822/25519
url http://hdl.handle.net/1822/25519
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 0168-1656
0168-1656
10.1016/j.jbiotec.2013.06.004
23774036
www.elsevier.com/locate/jbiotec
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
Elsevier BV
publisher.none.fl_str_mv Elsevier
Elsevier BV
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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