Emulsan–alginate beads for protein adsorption

Autores
Castro, Guillermo Raúl; Chen, Jingsong; Panilaitis, Bruce;; Kaplan, David L.;
Año de publicación
2012
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Emulsan–alginate beads were prepared and challenged using bovine serum albumin (BSA) to assess adsorption in comparison to alginate beads. BSA binding to the emulsan–alginate beads was improved over the alginate bead controls and protein adsorption was less sensitive to changes in ionic strength. BSA adsorption between pH 8.5 and 5.3 in alginate beads was 2–3-times lower compared to the emulsan–alginate beads in the same pH range. BSA adsorption and kinetic constants were at least 2-times higher for the emulsan–alginate beads compared to the alginate controls based on the Langmuir adsorption model. To further explore the utility of these novel emulsan–alginate bead systems, complex cell-free supernatants from some pathogenic microorganisms were exposed to the emulsan–alginate beads and increased protein adsorption was found when compared to controls. These trends were also confirmed with α-hemolysin toxicity studies. The data suggest that the protein-binding capacity of emulsan–alginate beads exceeds alginate controls, attributable to the unique binding features of emulsan.
Centro de Investigación y Desarrollo en Fermentaciones Industriales
Materia
Bioquímica
Adsorption
Alginate
Emulsan
Hydrogel
Biopolymer
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by-nc-sa/4.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/153005

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network_name_str SEDICI (UNLP)
spelling Emulsan–alginate beads for protein adsorptionCastro, Guillermo RaúlChen, JingsongPanilaitis, Bruce;Kaplan, David L.;BioquímicaAdsorptionAlginateEmulsanHydrogelBiopolymerEmulsan–alginate beads were prepared and challenged using bovine serum albumin (BSA) to assess adsorption in comparison to alginate beads. BSA binding to the emulsan–alginate beads was improved over the alginate bead controls and protein adsorption was less sensitive to changes in ionic strength. BSA adsorption between pH 8.5 and 5.3 in alginate beads was 2–3-times lower compared to the emulsan–alginate beads in the same pH range. BSA adsorption and kinetic constants were at least 2-times higher for the emulsan–alginate beads compared to the alginate controls based on the Langmuir adsorption model. To further explore the utility of these novel emulsan–alginate bead systems, complex cell-free supernatants from some pathogenic microorganisms were exposed to the emulsan–alginate beads and increased protein adsorption was found when compared to controls. These trends were also confirmed with α-hemolysin toxicity studies. The data suggest that the protein-binding capacity of emulsan–alginate beads exceeds alginate controls, attributable to the unique binding features of emulsan.Centro de Investigación y Desarrollo en Fermentaciones Industriales2012info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttp://sedici.unlp.edu.ar/handle/10915/153005enginfo:eu-repo/semantics/altIdentifier/issn/0920-5063info:eu-repo/semantics/altIdentifier/issn/1568-5624info:eu-repo/semantics/altIdentifier/doi/10.1163/156856209X416449info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-sa/4.0/Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-03T11:11:34Zoai:sedici.unlp.edu.ar:10915/153005Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-03 11:11:35.097SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv Emulsan–alginate beads for protein adsorption
title Emulsan–alginate beads for protein adsorption
spellingShingle Emulsan–alginate beads for protein adsorption
Castro, Guillermo Raúl
Bioquímica
Adsorption
Alginate
Emulsan
Hydrogel
Biopolymer
title_short Emulsan–alginate beads for protein adsorption
title_full Emulsan–alginate beads for protein adsorption
title_fullStr Emulsan–alginate beads for protein adsorption
title_full_unstemmed Emulsan–alginate beads for protein adsorption
title_sort Emulsan–alginate beads for protein adsorption
dc.creator.none.fl_str_mv Castro, Guillermo Raúl
Chen, Jingsong
Panilaitis, Bruce;
Kaplan, David L.;
author Castro, Guillermo Raúl
author_facet Castro, Guillermo Raúl
Chen, Jingsong
Panilaitis, Bruce;
Kaplan, David L.;
author_role author
author2 Chen, Jingsong
Panilaitis, Bruce;
Kaplan, David L.;
author2_role author
author
author
dc.subject.none.fl_str_mv Bioquímica
Adsorption
Alginate
Emulsan
Hydrogel
Biopolymer
topic Bioquímica
Adsorption
Alginate
Emulsan
Hydrogel
Biopolymer
dc.description.none.fl_txt_mv Emulsan–alginate beads were prepared and challenged using bovine serum albumin (BSA) to assess adsorption in comparison to alginate beads. BSA binding to the emulsan–alginate beads was improved over the alginate bead controls and protein adsorption was less sensitive to changes in ionic strength. BSA adsorption between pH 8.5 and 5.3 in alginate beads was 2–3-times lower compared to the emulsan–alginate beads in the same pH range. BSA adsorption and kinetic constants were at least 2-times higher for the emulsan–alginate beads compared to the alginate controls based on the Langmuir adsorption model. To further explore the utility of these novel emulsan–alginate bead systems, complex cell-free supernatants from some pathogenic microorganisms were exposed to the emulsan–alginate beads and increased protein adsorption was found when compared to controls. These trends were also confirmed with α-hemolysin toxicity studies. The data suggest that the protein-binding capacity of emulsan–alginate beads exceeds alginate controls, attributable to the unique binding features of emulsan.
Centro de Investigación y Desarrollo en Fermentaciones Industriales
description Emulsan–alginate beads were prepared and challenged using bovine serum albumin (BSA) to assess adsorption in comparison to alginate beads. BSA binding to the emulsan–alginate beads was improved over the alginate bead controls and protein adsorption was less sensitive to changes in ionic strength. BSA adsorption between pH 8.5 and 5.3 in alginate beads was 2–3-times lower compared to the emulsan–alginate beads in the same pH range. BSA adsorption and kinetic constants were at least 2-times higher for the emulsan–alginate beads compared to the alginate controls based on the Langmuir adsorption model. To further explore the utility of these novel emulsan–alginate bead systems, complex cell-free supernatants from some pathogenic microorganisms were exposed to the emulsan–alginate beads and increased protein adsorption was found when compared to controls. These trends were also confirmed with α-hemolysin toxicity studies. The data suggest that the protein-binding capacity of emulsan–alginate beads exceeds alginate controls, attributable to the unique binding features of emulsan.
publishDate 2012
dc.date.none.fl_str_mv 2012
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info:eu-repo/semantics/publishedVersion
Articulo
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format article
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dc.identifier.none.fl_str_mv http://sedici.unlp.edu.ar/handle/10915/153005
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language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/issn/0920-5063
info:eu-repo/semantics/altIdentifier/issn/1568-5624
info:eu-repo/semantics/altIdentifier/doi/10.1163/156856209X416449
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
dc.format.none.fl_str_mv application/pdf
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instname:Universidad Nacional de La Plata
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repository.name.fl_str_mv SEDICI (UNLP) - Universidad Nacional de La Plata
repository.mail.fl_str_mv alira@sedici.unlp.edu.ar
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