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dc.contributor.author
Santagapita, Patricio Roman
dc.contributor.author
Mazzobre, Maria Florencia
dc.contributor.author
Buera, Maria del Pilar
dc.date.available
2021-11-25T06:34:34Z
dc.date.issued
2019-03
dc.identifier.citation
Santagapita, Patricio Roman; Mazzobre, Maria Florencia; Buera, Maria del Pilar; Catalase Stability in Amorphous and Supercooled Media Related to Trehalose- Water- Salt Interactions; Springer; Food Biophysics; 14; 1; 3-2019; 90-96
dc.identifier.issn
1557-1858
dc.identifier.uri
http://hdl.handle.net/11336/147383
dc.description.abstract
Sugars are the most common excipients added to pharmaceutical and biotechnological formulations as protein protectants due to their adequate physicochemical properties, low toxicity, high purity and low cost. However, a second excipient is generally required to extend their protection in supercooled media. The effect of electrolytes is of special interest because of their universal presence in biological systems, their major influence on water structure, and their capability to interact with biomolecules. The purpose of the present work was to analyze the effect of different salts on the stability of catalase in amorphous (glassy and supercooled) trehalose matrices. Trehalose-Mg2+ system was better than trehalose alone to protect the enzyme both during freeze-drying and later storage at low RH (22%). The stabilizing effect observed for certain salts in these systems was not related with an increase of the Tg value. Under conditions at which trehalose crystallizes (43 %RH), salts (especially Mg2+) were detrimental since the enzyme became confined in a salt-concentrated region. Protein denaturation and aggregation were analyzed through differential scanning calorimetry in order to correlate activity changes with physical changes. Trehalose systems without salt and Mg2+-containing systems showed almost no aggregation after denaturation, in agreement with the thermal stability of the enzyme. Thus, the two major parameters related to enzyme stability in freeze-dried non-crystallized systems are: enzyme characteristics (type, quaternary structure) and salt-protein specific interactions.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Springer
dc.rights
info:eu-repo/semantics/restrictedAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
CATALASE
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CRYSTALLIZATION
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ENZYME STABILITY
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FREEZE-DRYING
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SALTS
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TREHALOSE
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Otras Biotecnología Industrial
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Biotecnología Industrial
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INGENIERÍAS Y TECNOLOGÍAS
dc.title
Catalase Stability in Amorphous and Supercooled Media Related to Trehalose- Water- Salt Interactions
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2020-11-25T17:59:15Z
dc.journal.volume
14
dc.journal.number
1
dc.journal.pagination
90-96
dc.journal.pais
Alemania
dc.description.fil
Fil: Santagapita, Patricio Roman. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias. Instituto de Tecnología de Alimentos y Procesos Químicos. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Tecnología de Alimentos y Procesos Químicos; Argentina
dc.description.fil
Fil: Mazzobre, Maria Florencia. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias. Instituto de Tecnología de Alimentos y Procesos Químicos. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Tecnología de Alimentos y Procesos Químicos; Argentina
dc.description.fil
Fil: Buera, Maria del Pilar. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias. Instituto de Tecnología de Alimentos y Procesos Químicos. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Tecnología de Alimentos y Procesos Químicos; Argentina
dc.journal.title
Food Biophysics
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://link.springer.com/10.1007/s11483-018-9560-5
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info:eu-repo/semantics/altIdentifier/doi/https://doi.org/10.1007/s11483-018-9560-5