Mostrar el registro sencillo del ítem

dc.contributor.author
Santagapita, Patricio Roman  
dc.contributor.author
Mazzobre, Maria Florencia  
dc.contributor.author
Cruz, Ariel García  
dc.contributor.author
Corti, Horacio Roberto  
dc.contributor.author
Villalonga, Reynaldo  
dc.contributor.author
Buera, Maria del Pilar  
dc.date.available
2019-06-10T18:47:17Z  
dc.date.issued
2013-05  
dc.identifier.citation
Santagapita, Patricio Roman; Mazzobre, Maria Florencia; Cruz, Ariel García; Corti, Horacio Roberto; Villalonga, Reynaldo; et al.; Polyethylene glycol-based low generation dendrimers functionalized with β-cyclodextrin as cryo- and dehydro-protectant of catalase formulations; American Chemical Society; Biotechnology Progress; 29; 3; 5-2013; 786-795  
dc.identifier.issn
1520-6033  
dc.identifier.uri
http://hdl.handle.net/11336/77869  
dc.description.abstract
Polyethylene glycol (PEG)-based low generation dendrimers are analyzed as single excipient or combined with trehalose in relation to their structure and efficiency as enzyme stabilizers during freeze-thawing, freeze-drying, and thermal treatment. A novel functional dendrimer (DG o -CD) based on the known PEG's ability as cryo-protector and β-CD as supramolecular stabilizing agent is presented. During freeze-thawing, PEG and β-CD failed to prevent catalase denaturation, while dendrimers, and especially DG o -CD, offered the better protection to the enzyme. During freeze-drying, trehalose was the best protective additive but DG o -CD provided also an adequate catalase stability showing a synergistic behavior in comparison to the activities recovered employing PEG or β-CD as unique additives. Although all the studied dendrimers improved the enzyme remaining activity during thermal treatment of freeze-dried formulations, the presence of amorphous trehalose was critical to enhance enzyme stability. The crystallinity of the protective matrix, either of PEG derivatives or of trehalose, negatively affected catalase stability in the freeze-dried systems. When humidified at 52% of relative humidity, the dendrimers delayed trehalose crystallization in the combined matrices, allowing extending the protection at those conditions in which normally trehalose fails. The results show how a relatively simple covalent combination of a polymer such as PEG with β-CD could significantly affect the properties of the individual components. Also, the results provide further insights about the role played by polymer-enzyme supramolecular interactions (host-guest crosslink, hydrogen bonding, and hydrophobic interactions) on enzyme stability in dehydrated models, being the effect on the stabilization also influenced by the physical state of the matrix. © 2013 American Institute of Chemical Engineers Biotechnol. © 2013 American Institute of Chemical Engineers.  
dc.format
application/pdf  
dc.language.iso
eng  
dc.publisher
American Chemical Society  
dc.rights
info:eu-repo/semantics/openAccess  
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/  
dc.subject
Β-Cyclodextrin  
dc.subject
Catalase  
dc.subject
Dehydration  
dc.subject
Dendrimer  
dc.subject
Enzyme Stability  
dc.subject
Freezing And Thawing, Peg  
dc.subject
Trehalose  
dc.subject.classification
Otras Ciencias Químicas  
dc.subject.classification
Ciencias Químicas  
dc.subject.classification
CIENCIAS NATURALES Y EXACTAS  
dc.title
Polyethylene glycol-based low generation dendrimers functionalized with β-cyclodextrin as cryo- and dehydro-protectant of catalase formulations  
dc.type
info:eu-repo/semantics/article  
dc.type
info:ar-repo/semantics/artículo  
dc.type
info:eu-repo/semantics/publishedVersion  
dc.date.updated
2019-06-10T14:27:27Z  
dc.identifier.eissn
8756-7938  
dc.journal.volume
29  
dc.journal.number
3  
dc.journal.pagination
786-795  
dc.journal.pais
Estados Unidos  
dc.journal.ciudad
Hoboken  
dc.description.fil
Fil: Santagapita, Patricio Roman. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias; Argentina  
dc.description.fil
Fil: Mazzobre, Maria Florencia. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias; Argentina  
dc.description.fil
Fil: Cruz, Ariel García. Universidad de Matanzas “Camilo Cienfuegos”; Cuba  
dc.description.fil
Fil: Corti, Horacio Roberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina. Comisión Nacional de Energía Atómica; Argentina  
dc.description.fil
Fil: Villalonga, Reynaldo. Universidad Complutense de Madrid; España  
dc.description.fil
Fil: Buera, Maria del Pilar. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Industrias; Argentina  
dc.journal.title
Biotechnology Progress  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://aiche.onlinelibrary.wiley.com/doi/abs/10.1002/btpr.1713  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1002/btpr.1713