Triggered release of proteins from emulsan–alginate beads

Autores
Castro, Guillermo Raul; 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 0.637F0.004 vs. 0.170F0.007 Ag/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.
Fil: Castro, Guillermo Raul. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; Argentina
Fil: Kamdar, Romit R.. Tufts University. School of Engineering; Estados Unidos
Fil: Panilaitis, Bruce. Tufts University. School of Engineering; Estados Unidos
Fil: Kaplan, David L.. Tufts University. School of Engineering; Estados Unidos
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/41718

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spelling Triggered release of proteins from emulsan–alginate beadsCastro, Guillermo RaulKamdar, Romit R.Panilaitis, BruceKaplan, David L.https://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1Emulsan/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 0.637F0.004 vs. 0.170F0.007 Ag/mg for beads formed from alginate alone. In additional protein adsorption experiments, the lipase and<br />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.Fil: Castro, Guillermo Raul. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; ArgentinaFil: Kamdar, Romit R.. Tufts University. School of Engineering; Estados UnidosFil: Panilaitis, Bruce. Tufts University. School of Engineering; Estados UnidosFil: Kaplan, David L.. Tufts University. School of Engineering; Estados UnidosElsevier Science2005-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/41718Castro, Guillermo Raul; Kamdar, Romit R.; Panilaitis, Bruce; Kaplan, David L.; Triggered release of proteins from emulsan–alginate beads; Elsevier Science; Journal of Controlled Release; 109; 1-3; 12-2005; 149-1570168-3659CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.jconrel.2005.09.042info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0168365905004888info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:44:13Zoai:ri.conicet.gov.ar:11336/41718instacron: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:34982025-09-03 09:44:13.75CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
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 Raul
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 Raul
Kamdar, Romit R.
Panilaitis, Bruce
Kaplan, David L.
author Castro, Guillermo Raul
author_facet Castro, Guillermo Raul
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
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
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 0.637F0.004 vs. 0.170F0.007 Ag/mg for beads formed from alginate alone. In additional protein adsorption experiments, the lipase and<br />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.
Fil: Castro, Guillermo Raul. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; Argentina
Fil: Kamdar, Romit R.. Tufts University. School of Engineering; Estados Unidos
Fil: Panilaitis, Bruce. Tufts University. School of Engineering; Estados Unidos
Fil: Kaplan, David L.. Tufts University. School of Engineering; Estados Unidos
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 0.637F0.004 vs. 0.170F0.007 Ag/mg for beads formed from alginate alone. In additional protein adsorption experiments, the lipase and<br />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 2005-12
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/11336/41718
Castro, Guillermo Raul; Kamdar, Romit R.; Panilaitis, Bruce; Kaplan, David L.; Triggered release of proteins from emulsan–alginate beads; Elsevier Science; Journal of Controlled Release; 109; 1-3; 12-2005; 149-157
0168-3659
CONICET Digital
CONICET
url http://hdl.handle.net/11336/41718
identifier_str_mv Castro, Guillermo Raul; Kamdar, Romit R.; Panilaitis, Bruce; Kaplan, David L.; Triggered release of proteins from emulsan–alginate beads; Elsevier Science; Journal of Controlled Release; 109; 1-3; 12-2005; 149-157
0168-3659
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.jconrel.2005.09.042
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0168365905004888
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv 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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