Triggered release of proteins from emulsan–alginate beads

Autores
Castro, Guillermo Raúl; Kamdar, Romit R.; Panilaitis, Bruce; Kaplan, David L.
Año de publicación
2005
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Emulsan/alginate beads were studied for protein adsorption and stability in the context of controlled release. The beads, 400F80 Am diameter with approximately 10% emulsan content, offer unusual opportunities for delivery of proteins due to the natural ability of emulsan to bind proteins, coupled with the selective biological activation features of this complex lipoheteropolysaccharide. The binding capacity of azo-bovine serum albumin by the emulsan/alginate beads was 0.637 ± 0.004 vs. 0.170 ± 0.007 μg/mg for beads formed from alginate alone. In additional protein adsorption experiments, the lipase and subtilisin maintained activity when adsorbed to the emulsan/alginate beads albeit with lower specific activity when compared to the enzyme free in solution. However, the half life of the adsorbed enzyme was significantly higher than the free forms. To explore functional utility of this system, two types of triggered release were studied in the context of these bead systems. First, azo-BSA as a model protein was physically bound to emulsan/alginate beads and then selectively released by triggering with subtilisin, a serine protease, which cleaves the azo dye, sulfanilic acid, from the bound protein. In absence of subtilisin no triggered release was observed. Second, azo-BSA as a prodrug model, was adsorbed to the emulsan/alginate beads and then release of the dye was demonstrated by lipase treatment which cleaves the fatty acid esters from the emulsan structure to release the bound protein. The results establish the versatility and utility of emulsan-based beads for protein binding and triggered release.
Centro de Investigación y Desarrollo en Fermentaciones Industriales
Materia
Bioquímica
Emulsan/alginate beads
controlled release
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:10915/153292

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network_name_str SEDICI (UNLP)
spelling Triggered release of proteins from emulsan–alginate beadsCastro, Guillermo RaúlKamdar, Romit R.Panilaitis, BruceKaplan, David L.BioquímicaEmulsan/alginate beadscontrolled releaseEmulsan/alginate beads were studied for protein adsorption and stability in the context of controlled release. The beads, 400F80 Am diameter with approximately 10% emulsan content, offer unusual opportunities for delivery of proteins due to the natural ability of emulsan to bind proteins, coupled with the selective biological activation features of this complex lipoheteropolysaccharide. The binding capacity of azo-bovine serum albumin by the emulsan/alginate beads was 0.637 ± 0.004 vs. 0.170 ± 0.007 μg/mg for beads formed from alginate alone. In additional protein adsorption experiments, the lipase and subtilisin maintained activity when adsorbed to the emulsan/alginate beads albeit with lower specific activity when compared to the enzyme free in solution. However, the half life of the adsorbed enzyme was significantly higher than the free forms. To explore functional utility of this system, two types of triggered release were studied in the context of these bead systems. First, azo-BSA as a model protein was physically bound to emulsan/alginate beads and then selectively released by triggering with subtilisin, a serine protease, which cleaves the azo dye, sulfanilic acid, from the bound protein. In absence of subtilisin no triggered release was observed. Second, azo-BSA as a prodrug model, was adsorbed to the emulsan/alginate beads and then release of the dye was demonstrated by lipase treatment which cleaves the fatty acid esters from the emulsan structure to release the bound protein. The results establish the versatility and utility of emulsan-based beads for protein binding and triggered release.Centro de Investigación y Desarrollo en Fermentaciones Industriales2005info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf149-157http://sedici.unlp.edu.ar/handle/10915/153292enginfo:eu-repo/semantics/altIdentifier/issn/0168-3659info:eu-repo/semantics/altIdentifier/issn/1873-4995info:eu-repo/semantics/altIdentifier/doi/10.1016/j.jconrel.2005.09.042info: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:UNLP2025-09-03T11:11:38Zoai:sedici.unlp.edu.ar:10915/153292Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-03 11:11:39.232SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv Triggered release of proteins from emulsan–alginate beads
title Triggered release of proteins from emulsan–alginate beads
spellingShingle Triggered release of proteins from emulsan–alginate beads
Castro, Guillermo Raúl
Bioquímica
Emulsan/alginate beads
controlled release
title_short Triggered release of proteins from emulsan–alginate beads
title_full Triggered release of proteins from emulsan–alginate beads
title_fullStr Triggered release of proteins from emulsan–alginate beads
title_full_unstemmed Triggered release of proteins from emulsan–alginate beads
title_sort Triggered release of proteins from emulsan–alginate beads
dc.creator.none.fl_str_mv Castro, Guillermo Raúl
Kamdar, Romit R.
Panilaitis, Bruce
Kaplan, David L.
author Castro, Guillermo Raúl
author_facet Castro, Guillermo Raúl
Kamdar, Romit R.
Panilaitis, Bruce
Kaplan, David L.
author_role author
author2 Kamdar, Romit R.
Panilaitis, Bruce
Kaplan, David L.
author2_role author
author
author
dc.subject.none.fl_str_mv Bioquímica
Emulsan/alginate beads
controlled release
topic Bioquímica
Emulsan/alginate beads
controlled release
dc.description.none.fl_txt_mv Emulsan/alginate beads were studied for protein adsorption and stability in the context of controlled release. The beads, 400F80 Am diameter with approximately 10% emulsan content, offer unusual opportunities for delivery of proteins due to the natural ability of emulsan to bind proteins, coupled with the selective biological activation features of this complex lipoheteropolysaccharide. The binding capacity of azo-bovine serum albumin by the emulsan/alginate beads was 0.637 ± 0.004 vs. 0.170 ± 0.007 μg/mg for beads formed from alginate alone. In additional protein adsorption experiments, the lipase and subtilisin maintained activity when adsorbed to the emulsan/alginate beads albeit with lower specific activity when compared to the enzyme free in solution. However, the half life of the adsorbed enzyme was significantly higher than the free forms. To explore functional utility of this system, two types of triggered release were studied in the context of these bead systems. First, azo-BSA as a model protein was physically bound to emulsan/alginate beads and then selectively released by triggering with subtilisin, a serine protease, which cleaves the azo dye, sulfanilic acid, from the bound protein. In absence of subtilisin no triggered release was observed. Second, azo-BSA as a prodrug model, was adsorbed to the emulsan/alginate beads and then release of the dye was demonstrated by lipase treatment which cleaves the fatty acid esters from the emulsan structure to release the bound protein. The results establish the versatility and utility of emulsan-based beads for protein binding and triggered release.
Centro de Investigación y Desarrollo en Fermentaciones Industriales
description Emulsan/alginate beads were studied for protein adsorption and stability in the context of controlled release. The beads, 400F80 Am diameter with approximately 10% emulsan content, offer unusual opportunities for delivery of proteins due to the natural ability of emulsan to bind proteins, coupled with the selective biological activation features of this complex lipoheteropolysaccharide. The binding capacity of azo-bovine serum albumin by the emulsan/alginate beads was 0.637 ± 0.004 vs. 0.170 ± 0.007 μg/mg for beads formed from alginate alone. In additional protein adsorption experiments, the lipase and subtilisin maintained activity when adsorbed to the emulsan/alginate beads albeit with lower specific activity when compared to the enzyme free in solution. However, the half life of the adsorbed enzyme was significantly higher than the free forms. To explore functional utility of this system, two types of triggered release were studied in the context of these bead systems. First, azo-BSA as a model protein was physically bound to emulsan/alginate beads and then selectively released by triggering with subtilisin, a serine protease, which cleaves the azo dye, sulfanilic acid, from the bound protein. In absence of subtilisin no triggered release was observed. Second, azo-BSA as a prodrug model, was adsorbed to the emulsan/alginate beads and then release of the dye was demonstrated by lipase treatment which cleaves the fatty acid esters from the emulsan structure to release the bound protein. The results establish the versatility and utility of emulsan-based beads for protein binding and triggered release.
publishDate 2005
dc.date.none.fl_str_mv 2005
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
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info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://sedici.unlp.edu.ar/handle/10915/153292
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dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/issn/0168-3659
info:eu-repo/semantics/altIdentifier/issn/1873-4995
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.jconrel.2005.09.042
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
149-157
dc.source.none.fl_str_mv reponame:SEDICI (UNLP)
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