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Glass transition and dynamics in BSA-water mixtures over wide ranges of composition studied by thermal and dielectric techniques

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Glass transition and dynamics in BSA-water mixtures over wide ranges of composition studied by thermal and dielectric techniques

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dc.contributor.author Panagopoulou, A. es_ES
dc.contributor.author Kyritsis, A. es_ES
dc.contributor.author Sabater i Serra, Roser es_ES
dc.contributor.author Gómez Ribelles, José Luís es_ES
dc.contributor.author Shinyashiki, N. es_ES
dc.contributor.author Pissis, P. es_ES
dc.date.accessioned 2014-01-10T10:20:13Z
dc.date.issued 2011
dc.identifier.issn 1570-9639
dc.identifier.uri http://hdl.handle.net/10251/34849
dc.description.abstract Protein-water dynamics in mixtures of water and a globular protein, bovine serum albumin (BSA), was studied over wide ranges of composition, in the form of solutions or hydrated solid pellets, by differential scanning calorimetry (DSC), thermally stimulated depolarization current technique (TSDC) and dielectric relaxation spectroscopy (DRS). Additionally, water equilibrium sorption isotherm (ESI) measurements were performed at room temperature. The crystallization and melting events were studied by DSC and the amount of uncrystallized water was calculated by the enthalpy of melting during heating. The glass transition of the system was detected by DSC for water contents higher than the critical water content corresponding to the formation of the first sorption layer of water molecules directly bound to primary hydration sites, namely 0.073 (grams of water per grams of dry protein), estimated by ESI. A strong plasticization of the Tg was observed by DSC for hydration levels lower than those necessary for crystallization of water during cooling, i.e. lower than about 0.3 (grams of water per grams of hydrated protein) followed by a stabilization of Tg at about - 80 °C for higher water contents. The ¿ relaxation associated with the glass transition was also observed in dielectric measurements. In TSDC a microphase separation could be detected resulting in double Tg for some hydration levels. A dielectric relaxation of small polar groups of the protein plasticized by water, overlapped by relaxations of uncrystallized water molecules, and a separate relaxation of water in the crystallized water phase (bulk ice crystals) were also recorded. © 2011 Elsevier B.V. All Rights Reserved. es_ES
dc.description.sponsorship JLGR acknowledges the support of the Spanish Ministry of Science and Innovation through project MAT2010-21611-C03-01 (including the FEDER financial support) and funding for research in the field of Regenerative Medicine through the collaboration agreement between the Conselleria de Sanidad (Generalitat Valenciana), and the Instituto de Salud Carlos III (Ministry of Science and Innovation). en_EN
dc.language Inglés es_ES
dc.publisher Elsevier es_ES
dc.relation.ispartof BBA - Proteins and Proteomics es_ES
dc.rights Reserva de todos los derechos es_ES
dc.subject Dielectric relaxation es_ES
dc.subject Glass transition es_ES
dc.subject Hydrated protein es_ES
dc.subject Molecular mobility es_ES
dc.subject Plasticization es_ES
dc.subject Uncrystallized water es_ES
dc.subject Bovine serum albumin es_ES
dc.subject Water es_ES
dc.subject Article es_ES
dc.subject Crystallization es_ES
dc.subject Differential scanning calorimetry es_ES
dc.subject Electrochemical impedance spectroscopy es_ES
dc.subject Glass transition temperature es_ES
dc.subject Priority journal es_ES
dc.subject Thermally stimulated luminescence es_ES
dc.subject Water content es_ES
dc.subject Animals es_ES
dc.subject Calorimetry, Differential Scanning es_ES
dc.subject Cattle es_ES
dc.subject Dielectric Spectroscopy es_ES
dc.subject Glass es_ES
dc.subject Kinetics es_ES
dc.subject Models, Biological es_ES
dc.subject Phase Transition es_ES
dc.subject Serum Albumin, Bovine es_ES
dc.subject Spectrometry, Mass, Electrospray Ionization es_ES
dc.subject Temperature es_ES
dc.subject Thermodynamics es_ES
dc.subject Bovinae es_ES
dc.subject.classification INGENIERIA ELECTRICA es_ES
dc.subject.classification MAQUINAS Y MOTORES TERMICOS es_ES
dc.title Glass transition and dynamics in BSA-water mixtures over wide ranges of composition studied by thermal and dielectric techniques es_ES
dc.type Artículo es_ES
dc.embargo.lift 10000-01-01
dc.embargo.terms forever es_ES
dc.identifier.doi 10.1016/j.bbapap.2011.07.014
dc.relation.projectID info:eu-repo/grantAgreement/MICINN//MAT2010-21611-C03-01/ES/MATERIALES BIOESTABLES Y BIOREABSORBIBLES A LARGO PLAZO COMO SOPORTES MACROPOROSOS PARA LA REGENERACION DEL CARTILAGO ARTICULAR/ es_ES
dc.rights.accessRights Cerrado es_ES
dc.contributor.affiliation Universitat Politècnica de València. Departamento de Termodinámica Aplicada - Departament de Termodinàmica Aplicada es_ES
dc.contributor.affiliation Universitat Politècnica de València. Departamento de Ingeniería Eléctrica - Departament d'Enginyeria Elèctrica es_ES
dc.description.bibliographicCitation Panagopoulou, A.; Kyritsis, A.; Sabater I Serra, R.; Gómez Ribelles, JL.; Shinyashiki, N.; Pissis, P. (2011). Glass transition and dynamics in BSA-water mixtures over wide ranges of composition studied by thermal and dielectric techniques. BBA - Proteins and Proteomics. 1814(12):1984-1996. https://doi.org/10.1016/j.bbapap.2011.07.014 es_ES
dc.description.accrualMethod S es_ES
dc.relation.publisherversion http://dx.doi.org/10.1016/j.bbapap.2011.07.014 es_ES
dc.description.upvformatpinicio 1984 es_ES
dc.description.upvformatpfin 1996 es_ES
dc.type.version info:eu-repo/semantics/publishedVersion es_ES
dc.description.volume 1814 es_ES
dc.description.issue 12 es_ES
dc.relation.senia 206849
dc.contributor.funder Ministerio de Ciencia e Innovación es_ES
dc.contributor.funder European Commission es_ES
dc.contributor.funder Generalitat Valenciana es_ES
dc.contributor.funder National Strategic Reference Framework, Grecia es_ES
dc.contributor.funder Instituto de Salud Carlos III es_ES


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