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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/41718
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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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1842268650700013568 |
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13.13397 |