Polyethylene glycol-based low generation dendrimers functionalized with β-cyclodextrin as cryo- and dehydro-protectant of catalase formulations
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 (DGo-CD) based on the kn...
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todo:paper_87567938_v29_n3_p786_Santagapita2023-10-03T16:42:35Z Polyethylene glycol-based low generation dendrimers functionalized with β-cyclodextrin as cryo- and dehydro-protectant of catalase formulations Santagapita, P.R. Mazzobre, M.F. Cruz, A.G. Corti, H.R. Villalonga, R. Buera, M.P. β-cyclodextrin Catalase Dehydration Dendrimer Enzyme stability Freezing and thawing, PEG Trehalose Catalase Enzyme stability Freeze-dried formulations Freezing and thawing Hydrophobic interactions Polyethylene glycol (PEG) Supramolecular interactions Trehalose Additives Dehydration Enzyme activity Heat treatment Hydrogen bonds Low temperature drying Models Polyethylene glycols Stabilization Supramolecular chemistry Thawing Dendrimers beta cyclodextrin derivative catalase dendrimer excipient macrogol derivative trehalose analysis of variance article chemistry drug effect enzyme stability freeze drying hydrodynamics particle size temperature Analysis of Variance beta-Cyclodextrins Catalase Dendrimers Enzyme Stability Excipients Freeze Drying Hydrodynamics Particle Size Polyethylene Glycols Temperature Trehalose 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 (DGo-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 DGo-CD, offered the better protection to the enzyme. During freeze-drying, trehalose was the best protective additive but DGo-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, P.R. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Mazzobre, M.F. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Corti, H.R. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Buera, M.P. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_87567938_v29_n3_p786_Santagapita |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
β-cyclodextrin Catalase Dehydration Dendrimer Enzyme stability Freezing and thawing, PEG Trehalose Catalase Enzyme stability Freeze-dried formulations Freezing and thawing Hydrophobic interactions Polyethylene glycol (PEG) Supramolecular interactions Trehalose Additives Dehydration Enzyme activity Heat treatment Hydrogen bonds Low temperature drying Models Polyethylene glycols Stabilization Supramolecular chemistry Thawing Dendrimers beta cyclodextrin derivative catalase dendrimer excipient macrogol derivative trehalose analysis of variance article chemistry drug effect enzyme stability freeze drying hydrodynamics particle size temperature Analysis of Variance beta-Cyclodextrins Catalase Dendrimers Enzyme Stability Excipients Freeze Drying Hydrodynamics Particle Size Polyethylene Glycols Temperature Trehalose |
| spellingShingle |
β-cyclodextrin Catalase Dehydration Dendrimer Enzyme stability Freezing and thawing, PEG Trehalose Catalase Enzyme stability Freeze-dried formulations Freezing and thawing Hydrophobic interactions Polyethylene glycol (PEG) Supramolecular interactions Trehalose Additives Dehydration Enzyme activity Heat treatment Hydrogen bonds Low temperature drying Models Polyethylene glycols Stabilization Supramolecular chemistry Thawing Dendrimers beta cyclodextrin derivative catalase dendrimer excipient macrogol derivative trehalose analysis of variance article chemistry drug effect enzyme stability freeze drying hydrodynamics particle size temperature Analysis of Variance beta-Cyclodextrins Catalase Dendrimers Enzyme Stability Excipients Freeze Drying Hydrodynamics Particle Size Polyethylene Glycols Temperature Trehalose Santagapita, P.R. Mazzobre, M.F. Cruz, A.G. Corti, H.R. Villalonga, R. Buera, M.P. Polyethylene glycol-based low generation dendrimers functionalized with β-cyclodextrin as cryo- and dehydro-protectant of catalase formulations |
| topic_facet |
β-cyclodextrin Catalase Dehydration Dendrimer Enzyme stability Freezing and thawing, PEG Trehalose Catalase Enzyme stability Freeze-dried formulations Freezing and thawing Hydrophobic interactions Polyethylene glycol (PEG) Supramolecular interactions Trehalose Additives Dehydration Enzyme activity Heat treatment Hydrogen bonds Low temperature drying Models Polyethylene glycols Stabilization Supramolecular chemistry Thawing Dendrimers beta cyclodextrin derivative catalase dendrimer excipient macrogol derivative trehalose analysis of variance article chemistry drug effect enzyme stability freeze drying hydrodynamics particle size temperature Analysis of Variance beta-Cyclodextrins Catalase Dendrimers Enzyme Stability Excipients Freeze Drying Hydrodynamics Particle Size Polyethylene Glycols Temperature Trehalose |
| 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 (DGo-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 DGo-CD, offered the better protection to the enzyme. During freeze-drying, trehalose was the best protective additive but DGo-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. |
| format |
JOUR |
| author |
Santagapita, P.R. Mazzobre, M.F. Cruz, A.G. Corti, H.R. Villalonga, R. Buera, M.P. |
| author_facet |
Santagapita, P.R. Mazzobre, M.F. Cruz, A.G. Corti, H.R. Villalonga, R. Buera, M.P. |
| author_sort |
Santagapita, P.R. |
| title |
Polyethylene glycol-based low generation dendrimers functionalized with β-cyclodextrin as cryo- and dehydro-protectant of catalase formulations |
| title_short |
Polyethylene glycol-based low generation dendrimers functionalized with β-cyclodextrin as cryo- and dehydro-protectant of catalase formulations |
| title_full |
Polyethylene glycol-based low generation dendrimers functionalized with β-cyclodextrin as cryo- and dehydro-protectant of catalase formulations |
| title_fullStr |
Polyethylene glycol-based low generation dendrimers functionalized with β-cyclodextrin as cryo- and dehydro-protectant of catalase formulations |
| title_full_unstemmed |
Polyethylene glycol-based low generation dendrimers functionalized with β-cyclodextrin as cryo- and dehydro-protectant of catalase formulations |
| title_sort |
polyethylene glycol-based low generation dendrimers functionalized with β-cyclodextrin as cryo- and dehydro-protectant of catalase formulations |
| url |
http://hdl.handle.net/20.500.12110/paper_87567938_v29_n3_p786_Santagapita |
| work_keys_str_mv |
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