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Glass transition and dynamics in lysozyme-water mixtures over wide ranges of composition

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Glass transition and dynamics in lysozyme-water mixtures over wide ranges of composition

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dc.contributor.author Panagopoulou, Anna es_ES
dc.contributor.author Kyritsis, Apostolos es_ES
dc.contributor.author Aravantinou, Anna-Maria es_ES
dc.contributor.author Nanopoulos, Dionysios es_ES
dc.contributor.author Sabater i Serra, Roser es_ES
dc.contributor.author Gómez Ribelles, José Luís es_ES
dc.contributor.author Shinyashiki, Naoki es_ES
dc.contributor.author Pissis, Polycarpos es_ES
dc.date.accessioned 2017-01-16T15:26:46Z
dc.date.available 2017-01-16T15:26:46Z
dc.date.issued 2011-06
dc.identifier.issn 1557-1858
dc.identifier.uri http://hdl.handle.net/10251/76889
dc.description.abstract [EN] Differential scanning calorimetry (DSC) and two dielectric techniques, broadband dielectric relaxation spectroscopy and thermally stimulated depolarization currents (TSDC), were employed to study glass transition and water and protein dynamics in mixtures of water and a globular protein, lysozyme, in wide ranges of water content, both solutions, and hydrated solid samples. In addition, water equilibrium sorption isotherms (ESI) measurements were performed at room temperature. The main objective was to correlate results by different techniques to each other and to determine critical water contents for various processes. From ESI measurements the content of water directly bound to primary hydration sites was determined to 0.088 (grams of water per grams of dry protein), corresponding to 71 water molecules per protein molecule, and that where clustering becomes significant to about 0.25. Crystallization and melting events of water were first observed at water contents 0.270 and 0.218, respectively, and the amount of uncrystallized water was found to increase with increasing water content. Two populations of ice crystals were observed by DSC, primary and bulk ice crystals, which give rise to two separate relaxations in dielectric measurements. In addition, the relaxation of uncrystallized water was observed, superimposed on a local relaxation of polar groups on the protein surface. The glass transition temperature, determined by DSC and TSDC in rather good agreement to each other, was found to decrease significantly with increasing water content and to stabilize at about −90 °C for water contents higher than about 0.25. This is a novel result of this study with potential impact on cryoprotection and pharmaceutics. es_ES
dc.description.sponsorship The research leading to these results has received funding from the European Community’s Seventh Framework Programme (FP7/2007–2013) under a Marie Curie International Research Staff Exchange Scheme, Grant Agreement No PIRSES-GA2008-230790.
dc.language Inglés es_ES
dc.publisher Springer Verlag (Germany) es_ES
dc.relation.ispartof Food Biophysics es_ES
dc.rights Reserva de todos los derechos es_ES
dc.subject Glass transition es_ES
dc.subject Molecular mobility es_ES
dc.subject Hydrated proteins es_ES
dc.subject Uncrystallized water es_ES
dc.subject Dielectric relaxation es_ES
dc.subject Plasticization 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 lysozyme-water mixtures over wide ranges of composition es_ES
dc.type Artículo es_ES
dc.identifier.doi 10.1007/s11483-010-9201-0
dc.relation.projectID info:eu-repo/grantAgreement/EC/FP7/230790/EU/Hybrid Nanocomposites and Their Applications/ es_ES
dc.rights.accessRights Cerrado es_ES
dc.contributor.affiliation Universitat Politècnica de València. Centro de Biomateriales e Ingeniería Tisular - Centre de Biomaterials i Enginyeria Tissular es_ES
dc.contributor.affiliation Universitat Politècnica de València. Escuela Técnica Superior de Ingenieros Industriales - Escola Tècnica Superior d'Enginyers Industrials es_ES
dc.contributor.affiliation Universitat Politècnica de València. Escuela Técnica Superior de Ingeniería del Diseño - Escola Tècnica Superior d'Enginyeria del Disseny es_ES
dc.description.bibliographicCitation Panagopoulou, A.; Kyritsis, A.; Aravantinou, A.; Nanopoulos, D.; Sabater I Serra, R.; Gómez Ribelles, JL.; Shinyashiki, N.... (2011). Glass transition and dynamics in lysozyme-water mixtures over wide ranges of composition. Food Biophysics. 6(2):199-209. https://doi.org/10.1007/s11483-010-9201-0 es_ES
dc.description.accrualMethod S es_ES
dc.relation.publisherversion http://dx.doi.org/10.1007/s11483-010-9201-0 es_ES
dc.description.upvformatpinicio 199 es_ES
dc.description.upvformatpfin 209 es_ES
dc.type.version info:eu-repo/semantics/publishedVersion es_ES
dc.description.volume 6 es_ES
dc.description.issue 2 es_ES
dc.relation.senia 206848 es_ES
dc.identifier.eissn 1557-1866
dc.contributor.funder European Commission
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