Protective role of trehalose on thermal stability of lactase in relation to its glass and crystal forming properties and effect of delaying crystallization

Thermal inactivation of β-galactosidase was investigated in dried matrices of poly(vinyl)pyrrolidone (PVP), maltodextrin and trehalose. Significant lactase inactivation was observed in the polymeric matrices kept well below their glass transition temperature (Tg). The stability of the enzyme in the...

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Detalles Bibliográficos
Autores principales: Mazzobre, María Florencia, Buera, María del Pilar
Publicado: 1997
Materias:
Trehalose; enzyme stability; lactase
Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00236438_v30_n3_p324_Mazzobre
http://hdl.handle.net/20.500.12110/paper_00236438_v30_n3_p324_Mazzobre
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
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spelling paper:paper_00236438_v30_n3_p324_Mazzobre2023-06-08T14:51:37Z Protective role of trehalose on thermal stability of lactase in relation to its glass and crystal forming properties and effect of delaying crystallization Mazzobre, María Florencia Buera, María del Pilar Trehalose; enzyme stability; lactase Thermal inactivation of β-galactosidase was investigated in dried matrices of poly(vinyl)pyrrolidone (PVP), maltodextrin and trehalose. Significant lactase inactivation was observed in the polymeric matrices kept well below their glass transition temperature (Tg). The stability of the enzyme in the anhydrous glassy matrices of maltodextrin and PVPs heated at 70 °C was directly related to their Tg; i.e. systems with higher glass transition temperature afforded better thermal protection of lactase. However, the stability of lactase in the heated trehalose matrix deviated from this behaviour since enzyme stability was higher than expected on the basis of the results obtained with polymeric matrices. In systems in which the trehalose matrix was rehumidified to conditions which allowed a high proportion of trehalose to crystallize, the enzyme was rapidly inactivated upon heating. Addition of maltodextrin to trehalose matrix provided enhanced protection to the enzyme, and this was probably due to delayed trehalose crystal formation. © 1997 Academic Press Limited. Fil:Mazzobre, M.F. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Del Pilar Buera, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 1997 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00236438_v30_n3_p324_Mazzobre http://hdl.handle.net/20.500.12110/paper_00236438_v30_n3_p324_Mazzobre
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic Trehalose; enzyme stability; lactase
spellingShingle Trehalose; enzyme stability; lactase
Mazzobre, María Florencia
Buera, María del Pilar
Protective role of trehalose on thermal stability of lactase in relation to its glass and crystal forming properties and effect of delaying crystallization
topic_facet Trehalose; enzyme stability; lactase
description Thermal inactivation of β-galactosidase was investigated in dried matrices of poly(vinyl)pyrrolidone (PVP), maltodextrin and trehalose. Significant lactase inactivation was observed in the polymeric matrices kept well below their glass transition temperature (Tg). The stability of the enzyme in the anhydrous glassy matrices of maltodextrin and PVPs heated at 70 °C was directly related to their Tg; i.e. systems with higher glass transition temperature afforded better thermal protection of lactase. However, the stability of lactase in the heated trehalose matrix deviated from this behaviour since enzyme stability was higher than expected on the basis of the results obtained with polymeric matrices. In systems in which the trehalose matrix was rehumidified to conditions which allowed a high proportion of trehalose to crystallize, the enzyme was rapidly inactivated upon heating. Addition of maltodextrin to trehalose matrix provided enhanced protection to the enzyme, and this was probably due to delayed trehalose crystal formation. © 1997 Academic Press Limited.
author Mazzobre, María Florencia
Buera, María del Pilar
author_facet Mazzobre, María Florencia
Buera, María del Pilar
author_sort Mazzobre, María Florencia
title Protective role of trehalose on thermal stability of lactase in relation to its glass and crystal forming properties and effect of delaying crystallization
title_short Protective role of trehalose on thermal stability of lactase in relation to its glass and crystal forming properties and effect of delaying crystallization
title_full Protective role of trehalose on thermal stability of lactase in relation to its glass and crystal forming properties and effect of delaying crystallization
title_fullStr Protective role of trehalose on thermal stability of lactase in relation to its glass and crystal forming properties and effect of delaying crystallization
title_full_unstemmed Protective role of trehalose on thermal stability of lactase in relation to its glass and crystal forming properties and effect of delaying crystallization
title_sort protective role of trehalose on thermal stability of lactase in relation to its glass and crystal forming properties and effect of delaying crystallization
publishDate 1997
url https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00236438_v30_n3_p324_Mazzobre
http://hdl.handle.net/20.500.12110/paper_00236438_v30_n3_p324_Mazzobre
work_keys_str_mv AT mazzobremariaflorencia protectiveroleoftrehaloseonthermalstabilityoflactaseinrelationtoitsglassandcrystalformingpropertiesandeffectofdelayingcrystallization
AT bueramariadelpilar protectiveroleoftrehaloseonthermalstabilityoflactaseinrelationtoitsglassandcrystalformingpropertiesandeffectofdelayingcrystallization
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