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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  
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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/openAccess  
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