Polyethylene glycol-based low generation dendrimers functionalized with β-cyclodextrin as cryo- and dehydro-protectant of catalase formulations

Authors
Santagapita, Patricio Roman; Mazzobre, Maria Florencia; Cruz, Ariel García; Corti, Horacio Roberto; Villalonga, Reynaldo; Buera, Maria del Pilar
Publication Year
2013
Language
English
Format
article
Status
Published version
Description
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.
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
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
Fil: Cruz, Ariel García. Universidad de Matanzas “Camilo Cienfuegos”; Cuba
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
Fil: Villalonga, Reynaldo. Universidad Complutense de Madrid; España
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
Subject
Β-CYCLODEXTRIN
CATALASE
DEHYDRATION
DENDRIMER
ENZYME STABILITY
FREEZING AND THAWING, PEG
TREHALOSE
Otras Ciencias Químicas
Ciencias Químicas
CIENCIAS NATURALES Y EXACTAS
Access level
Restricted access
License
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repository
CONICET Digital (CONICET)
Institution
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identifier
oai:ri.conicet.gov.ar:11336/77869