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

ilustraciones, gráficas, tablas

Autores:
Beltran Molina, Yuver Alejandro
Tipo de recurso:
Doctoral thesis
Fecha de publicación:
2021
Institución:
Universidad Nacional de Colombia
Repositorio:
Universidad Nacional de Colombia
Idioma:
spa
OAI Identifier:
oai:repositorio.unal.edu.co:unal/81465
Acceso en línea:
https://repositorio.unal.edu.co/handle/unal/81465
https://repositorio.unal.edu.co/
Palabra clave:
540 - Química y ciencias afines::542 - Técnicas, procedimientos, aparatos, equipos, materiales
Adsorption
Peptidase
Electrolyte solutions
Adsorción
Peptidasas
Soluciones electrolíticas
α-quimotripsinógeno
UV-Vis
DSC
Tensión superficial
Electrolitos
Interacción preferencial
α-chymotrypsinogen
UV-Vis
DSC
Surface tension
Electrolytes
Preferential interaction
Rights
openAccess
License
Reconocimiento 4.0 Internacional
id UNACIONAL2_20952f91538aa6ddd93eb12895299230
oai_identifier_str oai:repositorio.unal.edu.co:unal/81465
network_acronym_str UNACIONAL2
network_name_str Universidad Nacional de Colombia
repository_id_str
dc.title.spa.fl_str_mv Estudio de la estabilidad termodinámica de la proteína α-quimotripsinógeno en soluciones acuosas de electrolitos fuertes
dc.title.translated.eng.fl_str_mv Study of the thermodynamic stability of the α-chymotrypsinogen protein in aqueous solutions of strong electrolytes
title Estudio de la estabilidad termodinámica de la proteína α-quimotripsinógeno en soluciones acuosas de electrolitos fuertes
spellingShingle Estudio de la estabilidad termodinámica de la proteína α-quimotripsinógeno en soluciones acuosas de electrolitos fuertes
540 - Química y ciencias afines::542 - Técnicas, procedimientos, aparatos, equipos, materiales
Adsorption
Peptidase
Electrolyte solutions
Adsorción
Peptidasas
Soluciones electrolíticas
α-quimotripsinógeno
UV-Vis
DSC
Tensión superficial
Electrolitos
Interacción preferencial
α-chymotrypsinogen
UV-Vis
DSC
Surface tension
Electrolytes
Preferential interaction
title_short Estudio de la estabilidad termodinámica de la proteína α-quimotripsinógeno en soluciones acuosas de electrolitos fuertes
title_full Estudio de la estabilidad termodinámica de la proteína α-quimotripsinógeno en soluciones acuosas de electrolitos fuertes
title_fullStr Estudio de la estabilidad termodinámica de la proteína α-quimotripsinógeno en soluciones acuosas de electrolitos fuertes
title_full_unstemmed Estudio de la estabilidad termodinámica de la proteína α-quimotripsinógeno en soluciones acuosas de electrolitos fuertes
title_sort Estudio de la estabilidad termodinámica de la proteína α-quimotripsinógeno en soluciones acuosas de electrolitos fuertes
dc.creator.fl_str_mv Beltran Molina, Yuver Alejandro
dc.contributor.advisor.spa.fl_str_mv Romero Isaza, Carmen María
dc.contributor.author.spa.fl_str_mv Beltran Molina, Yuver Alejandro
dc.contributor.researchgroup.spa.fl_str_mv Grupo de Termodinámica Clásica
dc.subject.ddc.spa.fl_str_mv 540 - Química y ciencias afines::542 - Técnicas, procedimientos, aparatos, equipos, materiales
topic 540 - Química y ciencias afines::542 - Técnicas, procedimientos, aparatos, equipos, materiales
Adsorption
Peptidase
Electrolyte solutions
Adsorción
Peptidasas
Soluciones electrolíticas
α-quimotripsinógeno
UV-Vis
DSC
Tensión superficial
Electrolitos
Interacción preferencial
α-chymotrypsinogen
UV-Vis
DSC
Surface tension
Electrolytes
Preferential interaction
dc.subject.lemb.eng.fl_str_mv Adsorption
Peptidase
Electrolyte solutions
dc.subject.lemb.spa.fl_str_mv Adsorción
Peptidasas
Soluciones electrolíticas
dc.subject.proposal.spa.fl_str_mv α-quimotripsinógeno
UV-Vis
DSC
Tensión superficial
Electrolitos
Interacción preferencial
dc.subject.proposal.eng.fl_str_mv α-chymotrypsinogen
UV-Vis
DSC
Surface tension
Electrolytes
Preferential interaction
description ilustraciones, gráficas, tablas
publishDate 2021
dc.date.issued.none.fl_str_mv 2021
dc.date.accessioned.none.fl_str_mv 2022-05-31T19:39:04Z
dc.date.available.none.fl_str_mv 2022-05-31T19:39:04Z
dc.type.spa.fl_str_mv Trabajo de grado - Doctorado
dc.type.driver.spa.fl_str_mv info:eu-repo/semantics/doctoralThesis
dc.type.version.spa.fl_str_mv info:eu-repo/semantics/acceptedVersion
dc.type.coar.spa.fl_str_mv http://purl.org/coar/resource_type/c_db06
dc.type.content.spa.fl_str_mv Text
dc.type.redcol.spa.fl_str_mv http://purl.org/redcol/resource_type/TD
format http://purl.org/coar/resource_type/c_db06
status_str acceptedVersion
dc.identifier.uri.none.fl_str_mv https://repositorio.unal.edu.co/handle/unal/81465
dc.identifier.instname.spa.fl_str_mv Universidad Nacional de Colombia
dc.identifier.reponame.spa.fl_str_mv Repositorio Institucional Universidad Nacional de Colombia
dc.identifier.repourl.spa.fl_str_mv https://repositorio.unal.edu.co/
url https://repositorio.unal.edu.co/handle/unal/81465
https://repositorio.unal.edu.co/
identifier_str_mv Universidad Nacional de Colombia
Repositorio Institucional Universidad Nacional de Colombia
dc.language.iso.spa.fl_str_mv spa
language spa
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spelling Reconocimiento 4.0 Internacionalhttp://creativecommons.org/licenses/by/4.0/info:eu-repo/semantics/openAccesshttp://purl.org/coar/access_right/c_abf2Romero Isaza, Carmen Maríafb770e62e886e57e87d5668393243824Beltran Molina, Yuver Alejandro28c803a1b30224540d9cfca8c1286de1Grupo de Termodinámica Clásica2022-05-31T19:39:04Z2022-05-31T19:39:04Z2021https://repositorio.unal.edu.co/handle/unal/81465Universidad Nacional de ColombiaRepositorio Institucional Universidad Nacional de Colombiahttps://repositorio.unal.edu.co/ilustraciones, gráficas, tablasLa 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).The 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 DSCIncluye anexosDoctoradoDoctor en Ciencias - QuímicaTermodinámica de solucionesxix, 168 páginasapplication/pdfspaUniversidad Nacional de ColombiaBogotá - Ciencias - Doctorado en Ciencias - QuímicaDepartamento de QuímicaFacultad de CienciasBogotá, ColombiaUniversidad Nacional de Colombia - Sede Bogotá540 - Química y ciencias afines::542 - Técnicas, procedimientos, aparatos, equipos, materialesAdsorptionPeptidaseElectrolyte solutionsAdsorciónPeptidasasSoluciones electrolíticasα-quimotripsinógenoUV-VisDSCTensión superficialElectrolitosInteracción preferencialα-chymotrypsinogenUV-VisDSCSurface tensionElectrolytesPreferential interactionEstudio de la estabilidad termodinámica de la proteína α-quimotripsinógeno en soluciones acuosas de electrolitos fuertesStudy of the thermodynamic stability of the α-chymotrypsinogen protein in aqueous solutions of strong electrolytesTrabajo de grado - Doctoradoinfo:eu-repo/semantics/doctoralThesisinfo:eu-repo/semantics/acceptedVersionhttp://purl.org/coar/resource_type/c_db06Texthttp://purl.org/redcol/resource_type/TDC. 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Timasheff, Mechanism of protein stabilization by glycerol: preferential hydration in glycerol-water mixtures, Biochemistry. 20 (16) (1981) 4667–4676.BibliotecariosEstudiantesInvestigadoresMaestrosPúblico generalORIGINAL80350192.2022.pdf80350192.2022.pdfTesis de Doctorado en Ciencias - Químicaapplication/pdf2737978https://repositorio.unal.edu.co/bitstream/unal/81465/1/80350192.2022.pdf1a8dab61edd83cc05c394611eee2f085MD51LICENSElicense.txtlicense.txttext/plain; charset=utf-84074https://repositorio.unal.edu.co/bitstream/unal/81465/2/license.txt8153f7789df02f0a4c9e079953658ab2MD52THUMBNAIL80350192.2022.pdf.jpg80350192.2022.pdf.jpgGenerated Thumbnailimage/jpeg5301https://repositorio.unal.edu.co/bitstream/unal/81465/3/80350192.2022.pdf.jpg3aca301cfeaf4bd393df8b50514c519fMD53unal/81465oai:repositorio.unal.edu.co:unal/814652023-08-04 23:04:45.025Repositorio Institucional Universidad Nacional de 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EVESURBIFBPUiBMQSBTRUNSRVRBUsONQSBHRU5FUkFMLiAqTEEgVEVTSVMgQSBQVUJMSUNBUiBERUJFIFNFUiBMQSBWRVJTScOTTiBGSU5BTCBBUFJPQkFEQS4gCgpBbCBoYWNlciBjbGljIGVuIGVsIHNpZ3VpZW50ZSBib3TDs24sIHVzdGVkIGluZGljYSBxdWUgZXN0w6EgZGUgYWN1ZXJkbyBjb24gZXN0b3MgdMOpcm1pbm9zLiBTaSB0aWVuZSBhbGd1bmEgZHVkYSBzb2JyZSBsYSBsaWNlbmNpYSwgcG9yIGZhdm9yLCBjb250YWN0ZSBjb24gZWwgYWRtaW5pc3RyYWRvciBkZWwgc2lzdGVtYS4KClVOSVZFUlNJREFEIE5BQ0lPTkFMIERFIENPTE9NQklBIC0gw5psdGltYSBtb2RpZmljYWNpw7NuIDE5LzEwLzIwMjEK

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