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dc.contributor.author
Boeris, Valeria
dc.contributor.author
Capella, Laura Verónica
dc.contributor.author
Peres, Gisele
dc.contributor.author
Burgos, Martha Ines
dc.contributor.author
Da Silveira, Nádya Pesce
dc.contributor.author
Fidelio, Gerardo Daniel
dc.contributor.author
Picó, Guillermo Alfredo
dc.date.available
2016-09-09T20:59:26Z
dc.date.issued
2013-06
dc.identifier.citation
Boeris, Valeria; Capella, Laura Verónica; Peres, Gisele; Burgos, Martha Ines; Da Silveira, Nádya Pesce; et al.; Chymotrypsin - Eudragit Complex Formation; Springer; Biotechnology And Bioprocess Engineering; 18; 3; 6-2013; 538-545
dc.identifier.issn
1226-8372
dc.identifier.uri
http://hdl.handle.net/11336/7600
dc.description.abstract
Eudragit® L100 (EuL) and Eudragit® S100 (EuS) are synthetic polyanions differing on their electric charge density. They interact with chymotrypsin (ChTRP), a basic protein forming soluble and non-soluble complexes. The complex formation was studied by dynamic light scattering, isothermal titration calorimetry, native fluorescence emission, circular dichroism and thermodynamical thermal stability of the enzyme. EuS was able to bind 33 ChTRP molecules while EuL, 60. The binding of ChTRP to both Eu was slightly endothermic and the entropic factor was responsible for the soluble complexes formation. The ChTRP-Eu size increases with pH and the binding of ChTRP to Eu modifies the Eu hydrodynamic radium. The interaction of ChTRP with Eu did not modify its secondary or tertiary structure. The thermal stability of ChTRP was increased when it interacted with both Eu.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Springer
dc.rights
info:eu-repo/semantics/restrictedAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Eudragit
dc.subject
Chymotrypsin
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Polyelectrolytes
dc.subject
Calorimetry
dc.subject.classification
Físico-Química, Ciencia de los Polímeros, Electroquímica
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Ciencias Químicas
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CIENCIAS NATURALES Y EXACTAS
dc.title
Chymotrypsin - Eudragit Complex Formation
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2016-05-27T19:45:34Z
dc.journal.volume
18
dc.journal.number
3
dc.journal.pagination
538-545
dc.journal.pais
Estados Unidos
dc.journal.ciudad
Nueva York
dc.description.fil
Fil: Boeris, Valeria. Universidad Nacional de Rosario. Facultad de Cs.bioquimicas y Farmaceuticas. Departamento de Quimica y Fisica. Area Fisicoquimica; Argentina
dc.description.fil
Fil: Capella, Laura Verónica. Universidad Nacional de Rosario. Facultad de Cs.bioquimicas y Farmaceuticas. Departamento de Quimica y Fisica. Area Fisicoquimica; Argentina
dc.description.fil
Fil: Peres, Gisele. Universidade Federal Do Rio Grande Do Sul; Brasil
dc.description.fil
Fil: Burgos, Martha Ines. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones En Química Biológica de Córdoba (p); Argentina
dc.description.fil
Fil: Da Silveira, Nádya Pesce. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Departamento de Quimica Biológica; Argentina
dc.description.fil
Fil: Fidelio, Gerardo Daniel. Universidade Federal Do Rio Grande Do Sul; Brasil
dc.description.fil
Fil: Picó, Guillermo Alfredo. Universidad Nacional de Cordoba. Facultad de Cs.exactas Fisicas y Naturales. Departamento de Quimica. Catedra de Quimica Biologica; Argentina. Consejo Nacional de Investigaciones Cientificas y Tecnicas. Centro Cientifico Tecnol.conicet - Rosario. Instituto de Procesos Biotecnologicos y Quimicos Rosario; Argentina
dc.journal.title
Biotechnology And Bioprocess Engineering
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://link.springer.com/article/10.1007/s12257-012-0553-9
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1007/s12257-012-0553-9
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