Thermal stability of invertase in reduced-moisture amorphous matrices in relation to glassy state and trehalose crystallization

The thermal stability of enzyme invertase in reduced-moisture model systems of maltodextrin (MD), polyvinylpyrrolidone (PVP; MW 40,000) and trehalose heated at 90°C was studied. Significant invertase inactivation was observed in heated glassy PVP and MD systems kept well below their glass transition...

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Autores principales:	Cardona, Silvia T., Schebor, Carolina C., Buera, María del Pilar
Publicado:	1997
Materias:	Crystallization Glass transition Invertase Thermal inactivation Trehalose
Acceso en línea:	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00221147_v62_n1_p105_Cardona http://hdl.handle.net/20.500.12110/paper_00221147_v62_n1_p105_Cardona
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	paper:paper_00221147_v62_n1_p105_Cardona
record_format	dspace
spelling	paper:paper_00221147_v62_n1_p105_Cardona2023-06-08T14:46:16Z Thermal stability of invertase in reduced-moisture amorphous matrices in relation to glassy state and trehalose crystallization Cardona, Silvia T. Schebor, Carolina C. Buera, María del Pilar Crystallization Glass transition Invertase Thermal inactivation Trehalose The thermal stability of enzyme invertase in reduced-moisture model systems of maltodextrin (MD), polyvinylpyrrolidone (PVP; MW 40,000) and trehalose heated at 90°C was studied. Significant invertase inactivation was observed in heated glassy PVP and MD systems kept well below their glass transition temperature (T(g)), but the enzyme was fairly stable in rubbery trehalose systems. However, at moisture contents which allowed trehalose crystallization rapid thermal inactivation of invertase was observed. Invertase inactivation in heated PVP, MD and trehalose systems of reduced-moisture could not be predicted on the basis of glass transition and this was particularly true for trehalose. Conditions which would allow collapse of the systems and crystallization of trehalose were fairly well predicted based oil the estimated T(g) of model systems. Fil:Cardona, S. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Schebor, C. 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. 1997 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00221147_v62_n1_p105_Cardona http://hdl.handle.net/20.500.12110/paper_00221147_v62_n1_p105_Cardona
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	Crystallization Glass transition Invertase Thermal inactivation Trehalose
spellingShingle	Crystallization Glass transition Invertase Thermal inactivation Trehalose Cardona, Silvia T. Schebor, Carolina C. Buera, María del Pilar Thermal stability of invertase in reduced-moisture amorphous matrices in relation to glassy state and trehalose crystallization
topic_facet	Crystallization Glass transition Invertase Thermal inactivation Trehalose
description	The thermal stability of enzyme invertase in reduced-moisture model systems of maltodextrin (MD), polyvinylpyrrolidone (PVP; MW 40,000) and trehalose heated at 90°C was studied. Significant invertase inactivation was observed in heated glassy PVP and MD systems kept well below their glass transition temperature (T(g)), but the enzyme was fairly stable in rubbery trehalose systems. However, at moisture contents which allowed trehalose crystallization rapid thermal inactivation of invertase was observed. Invertase inactivation in heated PVP, MD and trehalose systems of reduced-moisture could not be predicted on the basis of glass transition and this was particularly true for trehalose. Conditions which would allow collapse of the systems and crystallization of trehalose were fairly well predicted based oil the estimated T(g) of model systems.
author	Cardona, Silvia T. Schebor, Carolina C. Buera, María del Pilar
author_facet	Cardona, Silvia T. Schebor, Carolina C. Buera, María del Pilar
author_sort	Cardona, Silvia T.
title	Thermal stability of invertase in reduced-moisture amorphous matrices in relation to glassy state and trehalose crystallization
title_short	Thermal stability of invertase in reduced-moisture amorphous matrices in relation to glassy state and trehalose crystallization
title_full	Thermal stability of invertase in reduced-moisture amorphous matrices in relation to glassy state and trehalose crystallization
title_fullStr	Thermal stability of invertase in reduced-moisture amorphous matrices in relation to glassy state and trehalose crystallization
title_full_unstemmed	Thermal stability of invertase in reduced-moisture amorphous matrices in relation to glassy state and trehalose crystallization
title_sort	thermal stability of invertase in reduced-moisture amorphous matrices in relation to glassy state and trehalose crystallization
publishDate	1997
url	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00221147_v62_n1_p105_Cardona http://hdl.handle.net/20.500.12110/paper_00221147_v62_n1_p105_Cardona
work_keys_str_mv	AT cardonasilviat thermalstabilityofinvertaseinreducedmoistureamorphousmatricesinrelationtoglassystateandtrehalosecrystallization AT scheborcarolinac thermalstabilityofinvertaseinreducedmoistureamorphousmatricesinrelationtoglassystateandtrehalosecrystallization AT bueramariadelpilar thermalstabilityofinvertaseinreducedmoistureamorphousmatricesinrelationtoglassystateandtrehalosecrystallization
_version_	1768543310122582016

Thermal stability of invertase in reduced-moisture amorphous matrices in relation to glassy state and trehalose crystallization

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