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, S., Schebor, C., Buera, M.P., Karel, M., Chirife, J.
Formato: JOUR
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Acceso en línea:http://hdl.handle.net/20.500.12110/paper_00221147_v62_n1_p105_Cardona
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spelling todo:paper_00221147_v62_n1_p105_Cardona2023-10-03T14:27:06Z Thermal stability of invertase in reduced-moisture amorphous matrices in relation to glassy state and trehalose crystallization Cardona, S. Schebor, C. Buera, M.P. Karel, M. Chirife, J. 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. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar 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, S.
Schebor, C.
Buera, M.P.
Karel, M.
Chirife, J.
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.
format JOUR
author Cardona, S.
Schebor, C.
Buera, M.P.
Karel, M.
Chirife, J.
author_facet Cardona, S.
Schebor, C.
Buera, M.P.
Karel, M.
Chirife, J.
author_sort Cardona, S.
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
url http://hdl.handle.net/20.500.12110/paper_00221147_v62_n1_p105_Cardona
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AT bueramp thermalstabilityofinvertaseinreducedmoistureamorphousmatricesinrelationtoglassystateandtrehalosecrystallization
AT karelm thermalstabilityofinvertaseinreducedmoistureamorphousmatricesinrelationtoglassystateandtrehalosecrystallization
AT chirifej thermalstabilityofinvertaseinreducedmoistureamorphousmatricesinrelationtoglassystateandtrehalosecrystallization
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