Analysis of the interaction of lipases with polypropylene of different structure and polypropylene-modified glass surface

Autores
Foresti, María Laura; Ferreira, María Luján
Año de publicación
2007
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The hydrophobic/hydrophilic characteristics of the surface exposed by a lipase support conditions the amount of adsorbed protein, and probably also the conformation of the immobilized lipase. In reference to polypropylene (PP) – hydrophobic – in this study the polymer obtained with metallocene catalysts (PPmet) showed the best characteristics for the immobilization of lipase from Candida antarctica B in terms of surface structure and particle size. On the other hand, commercial pellets of polypropylene obtained with Ziegler-Natta catalysts (PPZN) showed to have lower affinity for proteins, which we attribute to a combination of higher particle size and different exposed surface. Despite its high affinity for proteins, low mechanical resistance of PPmet prohibited its use as lipase support in reactive systems with high mechanical efforts, such as strongly magnetically stirred batch laboratory reactors. Coating of glass balls with the polymer was attempted in order to confer better mechanical properties to PPmet. Mixed surfaces of PPmet/glass balls pre-treated with an acid/base protocol to generate surface OH successfully allowed biocatalyst recovery and reuse. However, the hydrophobic–hydrophilic surface generated could not resemble the strong active protein bonding achieved with powdered metallocenic polypropylene. Lipase adsorption over uncovered glass regions is proposed to be the reason for the differences found.
Fil: Foresti, María Laura. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Planta Piloto de Ingeniería Química. Universidad Nacional del Sur. Planta Piloto de Ingeniería Química; Argentina
Fil: Ferreira, María Luján. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Planta Piloto de Ingeniería Química. Universidad Nacional del Sur. Planta Piloto de Ingeniería Química; Argentina
Materia
Adsorption
Exposed Surface
Glass
Lipase Support
Mechanical Resistance
Polypropylene
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/54976
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/54976
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Analysis of the interaction of lipases with polypropylene of different structure and polypropylene-modified glass surfaceForesti, María LauraFerreira, María LujánAdsorptionExposed SurfaceGlassLipase SupportMechanical ResistancePolypropylenehttps://purl.org/becyt/ford/2.4https://purl.org/becyt/ford/2The hydrophobic/hydrophilic characteristics of the surface exposed by a lipase support conditions the amount of adsorbed protein, and probably also the conformation of the immobilized lipase. In reference to polypropylene (PP) – hydrophobic – in this study the polymer obtained with metallocene catalysts (PPmet) showed the best characteristics for the immobilization of lipase from Candida antarctica B in terms of surface structure and particle size. On the other hand, commercial pellets of polypropylene obtained with Ziegler-Natta catalysts (PPZN) showed to have lower affinity for proteins, which we attribute to a combination of higher particle size and different exposed surface. Despite its high affinity for proteins, low mechanical resistance of PPmet prohibited its use as lipase support in reactive systems with high mechanical efforts, such as strongly magnetically stirred batch laboratory reactors. Coating of glass balls with the polymer was attempted in order to confer better mechanical properties to PPmet. Mixed surfaces of PPmet/glass balls pre-treated with an acid/base protocol to generate surface OH successfully allowed biocatalyst recovery and reuse. However, the hydrophobic–hydrophilic surface generated could not resemble the strong active protein bonding achieved with powdered metallocenic polypropylene. Lipase adsorption over uncovered glass regions is proposed to be the reason for the differences found.Fil: Foresti, María Laura. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Planta Piloto de Ingeniería Química. Universidad Nacional del Sur. Planta Piloto de Ingeniería Química; ArgentinaFil: Ferreira, María Luján. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Planta Piloto de Ingeniería Química. Universidad Nacional del Sur. Planta Piloto de Ingeniería Química; ArgentinaElsevier Science2007-02info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/54976Foresti, María Laura; Ferreira, María Luján; Analysis of the interaction of lipases with polypropylene of different structure and polypropylene-modified glass surface; Elsevier Science; Colloids and Surfaces A: Physicochemical and Engineering Aspects; 294; 1-3; 2-2007; 147-1550927-7757CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.colsurfa.2006.08.009info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0927775706006182info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:36:00Zoai:ri.conicet.gov.ar:11336/54976instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 09:36:00.477CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Analysis of the interaction of lipases with polypropylene of different structure and polypropylene-modified glass surface
title Analysis of the interaction of lipases with polypropylene of different structure and polypropylene-modified glass surface
spellingShingle Analysis of the interaction of lipases with polypropylene of different structure and polypropylene-modified glass surface
Foresti, María Laura
Adsorption
Exposed Surface
Glass
Lipase Support
Mechanical Resistance
Polypropylene
title_short Analysis of the interaction of lipases with polypropylene of different structure and polypropylene-modified glass surface
title_full Analysis of the interaction of lipases with polypropylene of different structure and polypropylene-modified glass surface
title_fullStr Analysis of the interaction of lipases with polypropylene of different structure and polypropylene-modified glass surface
title_full_unstemmed Analysis of the interaction of lipases with polypropylene of different structure and polypropylene-modified glass surface
title_sort Analysis of the interaction of lipases with polypropylene of different structure and polypropylene-modified glass surface
dc.creator.none.fl_str_mv Foresti, María Laura
Ferreira, María Luján
author Foresti, María Laura
author_facet Foresti, María Laura
Ferreira, María Luján
author_role author
author2 Ferreira, María Luján
author2_role author
dc.subject.none.fl_str_mv Adsorption
Exposed Surface
Glass
Lipase Support
Mechanical Resistance
Polypropylene
topic Adsorption
Exposed Surface
Glass
Lipase Support
Mechanical Resistance
Polypropylene
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.4
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv The hydrophobic/hydrophilic characteristics of the surface exposed by a lipase support conditions the amount of adsorbed protein, and probably also the conformation of the immobilized lipase. In reference to polypropylene (PP) – hydrophobic – in this study the polymer obtained with metallocene catalysts (PPmet) showed the best characteristics for the immobilization of lipase from Candida antarctica B in terms of surface structure and particle size. On the other hand, commercial pellets of polypropylene obtained with Ziegler-Natta catalysts (PPZN) showed to have lower affinity for proteins, which we attribute to a combination of higher particle size and different exposed surface. Despite its high affinity for proteins, low mechanical resistance of PPmet prohibited its use as lipase support in reactive systems with high mechanical efforts, such as strongly magnetically stirred batch laboratory reactors. Coating of glass balls with the polymer was attempted in order to confer better mechanical properties to PPmet. Mixed surfaces of PPmet/glass balls pre-treated with an acid/base protocol to generate surface OH successfully allowed biocatalyst recovery and reuse. However, the hydrophobic–hydrophilic surface generated could not resemble the strong active protein bonding achieved with powdered metallocenic polypropylene. Lipase adsorption over uncovered glass regions is proposed to be the reason for the differences found.
Fil: Foresti, María Laura. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Planta Piloto de Ingeniería Química. Universidad Nacional del Sur. Planta Piloto de Ingeniería Química; Argentina
Fil: Ferreira, María Luján. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Planta Piloto de Ingeniería Química. Universidad Nacional del Sur. Planta Piloto de Ingeniería Química; Argentina
description The hydrophobic/hydrophilic characteristics of the surface exposed by a lipase support conditions the amount of adsorbed protein, and probably also the conformation of the immobilized lipase. In reference to polypropylene (PP) – hydrophobic – in this study the polymer obtained with metallocene catalysts (PPmet) showed the best characteristics for the immobilization of lipase from Candida antarctica B in terms of surface structure and particle size. On the other hand, commercial pellets of polypropylene obtained with Ziegler-Natta catalysts (PPZN) showed to have lower affinity for proteins, which we attribute to a combination of higher particle size and different exposed surface. Despite its high affinity for proteins, low mechanical resistance of PPmet prohibited its use as lipase support in reactive systems with high mechanical efforts, such as strongly magnetically stirred batch laboratory reactors. Coating of glass balls with the polymer was attempted in order to confer better mechanical properties to PPmet. Mixed surfaces of PPmet/glass balls pre-treated with an acid/base protocol to generate surface OH successfully allowed biocatalyst recovery and reuse. However, the hydrophobic–hydrophilic surface generated could not resemble the strong active protein bonding achieved with powdered metallocenic polypropylene. Lipase adsorption over uncovered glass regions is proposed to be the reason for the differences found.
publishDate 2007
dc.date.none.fl_str_mv 2007-02
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/54976
Foresti, María Laura; Ferreira, María Luján; Analysis of the interaction of lipases with polypropylene of different structure and polypropylene-modified glass surface; Elsevier Science; Colloids and Surfaces A: Physicochemical and Engineering Aspects; 294; 1-3; 2-2007; 147-155
0927-7757
CONICET Digital
CONICET
url http://hdl.handle.net/11336/54976
identifier_str_mv Foresti, María Laura; Ferreira, María Luján; Analysis of the interaction of lipases with polypropylene of different structure and polypropylene-modified glass surface; Elsevier Science; Colloids and Surfaces A: Physicochemical and Engineering Aspects; 294; 1-3; 2-2007; 147-155
0927-7757
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1016/j.colsurfa.2006.08.009
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0927775706006182
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier Science
publisher.none.fl_str_mv Elsevier Science
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.070432

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