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Estudio de la estabilidad termodinámica de la proteína α-quimotripsinógeno en soluciones acuosas de electrolitos fuertes

dc.rights.licenseReconocimiento 4.0 Internacional
dc.contributor.advisorRomero Isaza, Carmen María
dc.contributor.authorBeltran Molina, Yuver Alejandro
dc.date.accessioned2022-05-31T19:39:04Z
dc.date.available2022-05-31T19:39:04Z
dc.date.issued2021
dc.identifier.urihttps://repositorio.unal.edu.co/handle/unal/81465
dc.descriptionilustraciones, gráficas, tablas
dc.description.abstractLa estabilidad termodinámica del α-quimotripsinógeno A, a pH 2,00, 3,00, 3,50 y en soluciones acuosas de los electrolitos NaCl, KCl, NH4NO3 y (NH4)2SO4 fue analizada por espectroscopía UV-Vis, calorimetría diferencial de barrido (DSC), tensión superficial y por medio de los parámetros de interacción preferencial determinados a partir de medidas de densidad. Los resultados obtenidos a partir de medidas de UV-Vis y DSC determinaron que el aumento en la estabilidad del α-quimotripsinógeno está relacionado con el aumento en la concentración de electrolito y con el aumento del pH. El efecto estabilizante que ejercen las sales sobre la estructura de la proteína aumenta en el siguiente orden: NaCl < NH4NO3 < KCl < (NH4)2SO4 A partir del estudio cinético de adsorción de la proteína en la interfase líquido/aire se determinó que este proceso se puede describir mediante un modelo de tres etapas y los valores obtenidos de la constante cinética k1 indicaron que el paso que controla el proceso de adsorción es la penetración y adsorción de la proteína en la interfase y que este paso es dependiente de la naturaleza y la concentración de las sales. Los resultados obtenidos para los parámetros de interacción preferencial indicaron que todos los electrolitos empleados en este estudio son excluidos de la superficie de la proteína y generan una hidratación preferencial que involucra un aumento en la estabilidad de la estructura nativa del α-quimotripsinógeno. Los resultados presentaron la misma tendencia que los obtenidos a partir de UV-Vis y DSC. (Texto tomado de la fuente).
dc.description.abstractThe thermodynamic stability of α-chymotrypsinogen A, at pH 2.00, 3.00, 3.50 and in aqueous solutions of the electrolytes NaCl, KCl, NH4NO3, and (NH4)2SO4 was analyzed by UV-Vis spectroscopy, differential scanning calorimetry (DSC), surface tension and through the preferential interaction parameters determined from density measurements. The results obtained from UV-Vis and DSC measurements determined that the increase in the stability of α-chymotrypsinogen is related to the increase in the electrolyte concentration as well as the increase in pH. The stabilizing effect of salts on protein structure increases in the following order: NaCl < NH4NO3 < KCl < (NH4)2SO4 From the kinetic study of protein adsorption at the liquid/air interface, it was determined that this process can be described by a three-stage model and the values obtained from the kinetic constant k1 indicate that the step that controls the adsorption process is the protein penetration and adsorption at the interface and this step is dependent on the nature and concentration of the salts. The results obtained for the preferential interaction parameters indicate that all the electrolytes used in this study were excluded from the surface of the protein and generated preferential hydration that involves an increase in the stability of the native structure of α-chymotrypsinogen. The results presented follow the same trend as those obtained from UV-Vis and DSC
dc.format.extentxix, 168 páginas
dc.format.mimetypeapplication/pdf
dc.language.isospa
dc.publisherUniversidad Nacional de Colombia
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/
dc.subject.ddc540 - Química y ciencias afines::542 - Técnicas, procedimientos, aparatos, equipos, materiales
dc.titleEstudio de la estabilidad termodinámica de la proteína α-quimotripsinógeno en soluciones acuosas de electrolitos fuertes
dc.typeTrabajo de grado - Doctorado
dc.type.driverinfo:eu-repo/semantics/doctoralThesis
dc.type.versioninfo:eu-repo/semantics/acceptedVersion
dc.publisher.programBogotá - Ciencias - Doctorado en Ciencias - Química
dc.description.notesIncluye anexos
dc.contributor.researchgroupGrupo de Termodinámica Clásica
dc.description.degreelevelDoctorado
dc.description.degreenameDoctor en Ciencias - Química
dc.description.researchareaTermodinámica de soluciones
dc.identifier.instnameUniversidad Nacional de Colombia
dc.identifier.reponameRepositorio Institucional Universidad Nacional de Colombia
dc.identifier.repourlhttps://repositorio.unal.edu.co/
dc.publisher.departmentDepartamento de Química
dc.publisher.facultyFacultad de Ciencias
dc.publisher.placeBogotá, Colombia
dc.publisher.branchUniversidad Nacional de Colombia - Sede Bogotá
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dc.rights.accessrightsinfo:eu-repo/semantics/openAccess
dc.subject.lembAdsorption
dc.subject.lembAdsorción
dc.subject.lembPeptidase
dc.subject.lembPeptidasas
dc.subject.lembElectrolyte solutions
dc.subject.lembSoluciones electrolíticas
dc.subject.proposalα-quimotripsinógeno
dc.subject.proposalUV-Vis
dc.subject.proposalDSC
dc.subject.proposalα-chymotrypsinogen
dc.subject.proposalUV-Vis
dc.subject.proposalDSC
dc.subject.proposalTensión superficial
dc.subject.proposalElectrolitos
dc.subject.proposalInteracción preferencial
dc.subject.proposalSurface tension
dc.subject.proposalElectrolytes
dc.subject.proposalPreferential interaction
dc.title.translatedStudy of the thermodynamic stability of the α-chymotrypsinogen protein in aqueous solutions of strong electrolytes
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dc.type.redcolhttp://purl.org/redcol/resource_type/TD
oaire.accessrightshttp://purl.org/coar/access_right/c_abf2
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