Glassy state in relation to the thermal inactivation of the enzyme invertase in amorphous dried matrices of trehalose, maltodextrin and PVP

The stabilization of invertase by its incorporation in aqueous trehalose and polymer solutions, followed by freeze-drying and desiccation to 'zero' moisture content, was studied. The dried amorphous preparations of trehalose, maltodextrin (MD; DE = 10·9), and poly(vinyl)pyrrolidone (PVP),...

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Autores principales: Schebor, Carolina C., Buera, María del Pilar
Publicado: 1996
Materias:
Amorphous materials
Glass transition
High temperature effects
Maltodrexin
Polyvinylpyrrolidone (PVP)
Trehalose
Enzyme immobilization
Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_02608774_v30_n3-4_p269_Schebor
http://hdl.handle.net/20.500.12110/paper_02608774_v30_n3-4_p269_Schebor
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Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
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spelling paper:paper_02608774_v30_n3-4_p269_Schebor2023-06-08T15:22:26Z Glassy state in relation to the thermal inactivation of the enzyme invertase in amorphous dried matrices of trehalose, maltodextrin and PVP Schebor, Carolina C. Buera, María del Pilar Amorphous materials Glass transition High temperature effects Maltodrexin Polyvinylpyrrolidone (PVP) Trehalose Enzyme immobilization The stabilization of invertase by its incorporation in aqueous trehalose and polymer solutions, followed by freeze-drying and desiccation to 'zero' moisture content, was studied. The dried amorphous preparations of trehalose, maltodextrin (MD; DE = 10·9), and poly(vinyl)pyrrolidone (PVP), molecular weights 360000, 40000 and 10000, greatly protected invertase - as compared with its behavior in liquid solution - from heat inactivation at elevated temperatures. Significant invertase inactivation was observed in heated PVP and MD matrices kept well below their glass-transition temperature. Under glassy conditions the extent of enzyme protection by MD and PVP systems was related to their glass-transition temperature (Tg) since systems of higher Tg afforded better protection. However, the data for trehalose deviated from this behavior since invertase stabilization was higher than expected on the basis of the results obtained with polymer matrices. Present results suggest that invertase inactivation in dried amorphous systems cannot be adequately explained by the glass-transition theory and this is particularly true for trehalose, for which some additional mechanism of enzyme protection is likely to operate. Copyright © 1996 Elsevier Science Limited. Fil:Schebor, C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Buera, M.D.P. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 1996 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_02608774_v30_n3-4_p269_Schebor http://hdl.handle.net/20.500.12110/paper_02608774_v30_n3-4_p269_Schebor
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic Amorphous materials
Glass transition
High temperature effects
Maltodrexin
Polyvinylpyrrolidone (PVP)
Trehalose
Enzyme immobilization
spellingShingle Amorphous materials
Glass transition
High temperature effects
Maltodrexin
Polyvinylpyrrolidone (PVP)
Trehalose
Enzyme immobilization
Schebor, Carolina C.
Buera, María del Pilar
Glassy state in relation to the thermal inactivation of the enzyme invertase in amorphous dried matrices of trehalose, maltodextrin and PVP
topic_facet Amorphous materials
Glass transition
High temperature effects
Maltodrexin
Polyvinylpyrrolidone (PVP)
Trehalose
Enzyme immobilization
description The stabilization of invertase by its incorporation in aqueous trehalose and polymer solutions, followed by freeze-drying and desiccation to 'zero' moisture content, was studied. The dried amorphous preparations of trehalose, maltodextrin (MD; DE = 10·9), and poly(vinyl)pyrrolidone (PVP), molecular weights 360000, 40000 and 10000, greatly protected invertase - as compared with its behavior in liquid solution - from heat inactivation at elevated temperatures. Significant invertase inactivation was observed in heated PVP and MD matrices kept well below their glass-transition temperature. Under glassy conditions the extent of enzyme protection by MD and PVP systems was related to their glass-transition temperature (Tg) since systems of higher Tg afforded better protection. However, the data for trehalose deviated from this behavior since invertase stabilization was higher than expected on the basis of the results obtained with polymer matrices. Present results suggest that invertase inactivation in dried amorphous systems cannot be adequately explained by the glass-transition theory and this is particularly true for trehalose, for which some additional mechanism of enzyme protection is likely to operate. Copyright © 1996 Elsevier Science Limited.
author Schebor, Carolina C.
Buera, María del Pilar
author_facet Schebor, Carolina C.
Buera, María del Pilar
author_sort Schebor, Carolina C.
title Glassy state in relation to the thermal inactivation of the enzyme invertase in amorphous dried matrices of trehalose, maltodextrin and PVP
title_short Glassy state in relation to the thermal inactivation of the enzyme invertase in amorphous dried matrices of trehalose, maltodextrin and PVP
title_full Glassy state in relation to the thermal inactivation of the enzyme invertase in amorphous dried matrices of trehalose, maltodextrin and PVP
title_fullStr Glassy state in relation to the thermal inactivation of the enzyme invertase in amorphous dried matrices of trehalose, maltodextrin and PVP
title_full_unstemmed Glassy state in relation to the thermal inactivation of the enzyme invertase in amorphous dried matrices of trehalose, maltodextrin and PVP
title_sort glassy state in relation to the thermal inactivation of the enzyme invertase in amorphous dried matrices of trehalose, maltodextrin and pvp
publishDate 1996
url https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_02608774_v30_n3-4_p269_Schebor
http://hdl.handle.net/20.500.12110/paper_02608774_v30_n3-4_p269_Schebor
work_keys_str_mv AT scheborcarolinac glassystateinrelationtothethermalinactivationoftheenzymeinvertaseinamorphousdriedmatricesoftrehalosemaltodextrinandpvp
AT bueramariadelpilar glassystateinrelationtothethermalinactivationoftheenzymeinvertaseinamorphousdriedmatricesoftrehalosemaltodextrinandpvp
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