Analysis of the interaction of lipases with polypropylene of different structure and polypropylene-modified glass surface
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 catal...
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ftconicet:oai:ri.conicet.gov.ar:11336/54976 2023-10-09T21:46:45+02:00 Analysis of the interaction of lipases with polypropylene of different structure and polypropylene-modified glass surface Foresti, María Laura Ferreira, María Luján application/pdf http://hdl.handle.net/11336/54976 eng eng Elsevier Science 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 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 info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-nd/2.5/ar/ Adsorption Exposed Surface Glass Lipase Support Mechanical Resistance Polypropylene https://purl.org/becyt/ford/2.4 https://purl.org/becyt/ford/2 info:eu-repo/semantics/article info:ar-repo/semantics/artículo info:eu-repo/semantics/publishedVersion ftconicet https://doi.org/10.1016/j.colsurfa.2006.08.009 2023-09-24T18:25:04Z 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 Article in Journal/Newspaper Antarc* Antarctica CONICET Digital (Consejo Nacional de Investigaciones Científicas y Técnicas) Argentina Ferreira ENVELOPE(-62.050,-62.050,-64.600,-64.600) Colloids and Surfaces A: Physicochemical and Engineering Aspects 294 1-3 147 155 |
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Open Polar |
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CONICET Digital (Consejo Nacional de Investigaciones Científicas y Técnicas) |
op_collection_id |
ftconicet |
language |
English |
topic |
Adsorption Exposed Surface Glass Lipase Support Mechanical Resistance Polypropylene https://purl.org/becyt/ford/2.4 https://purl.org/becyt/ford/2 |
spellingShingle |
Adsorption Exposed Surface Glass Lipase Support Mechanical Resistance Polypropylene https://purl.org/becyt/ford/2.4 https://purl.org/becyt/ford/2 Foresti, María Laura Ferreira, María Luján Analysis of the interaction of lipases with polypropylene of different structure and polypropylene-modified glass surface |
topic_facet |
Adsorption Exposed Surface Glass Lipase Support Mechanical Resistance Polypropylene https://purl.org/becyt/ford/2.4 https://purl.org/becyt/ford/2 |
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. 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 |
format |
Article in Journal/Newspaper |
author |
Foresti, María Laura Ferreira, María Luján |
author_facet |
Foresti, María Laura Ferreira, María Luján |
author_sort |
Foresti, María Laura |
title |
Analysis of the interaction of lipases with polypropylene of different structure and polypropylene-modified glass surface |
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 |
publisher |
Elsevier Science |
url |
http://hdl.handle.net/11336/54976 |
long_lat |
ENVELOPE(-62.050,-62.050,-64.600,-64.600) |
geographic |
Argentina Ferreira |
geographic_facet |
Argentina Ferreira |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_relation |
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 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 |
op_rights |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-nd/2.5/ar/ |
op_doi |
https://doi.org/10.1016/j.colsurfa.2006.08.009 |
container_title |
Colloids and Surfaces A: Physicochemical and Engineering Aspects |
container_volume |
294 |
container_issue |
1-3 |
container_start_page |
147 |
op_container_end_page |
155 |
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1779309257613639680 |