Thermal resistance of β-galactosidase in dehydrated dairy model systems as affected by physical and chemical changes

The objective was to study the remaining activity of the enzyme β-galactosidase in dehydrated dairy systems and its relationship with simultaneous chemical (i.e. non-enzymatic browning, NEB) and physical changes (structural collapse) at temperatures from 70 to 105°C. The presence of milk proteins ha...

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Autores principales: Burin, L., Buera, M.P., Hough, G., Chirife, J.
Formato: JOUR
Materias:
β-galactosidase
Dehydrated dairy products
Enzyme stability
Glass transition
Non enzymatic browning: Collapse
beta galactosidase
lactose
milk protein
article
dairy product
dehydration
enzyme activity
enzyme inactivation
enzyme stability
heat tolerance
physical chemistry
storage temperature
temperature
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_03088146_v76_n4_p423_Burin
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
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spelling todo:paper_03088146_v76_n4_p423_Burin2023-10-03T15:22:59Z Thermal resistance of β-galactosidase in dehydrated dairy model systems as affected by physical and chemical changes Burin, L. Buera, M.P. Hough, G. Chirife, J. β-galactosidase Dehydrated dairy products Enzyme stability Glass transition Non enzymatic browning: Collapse beta galactosidase lactose milk protein article dairy product dehydration enzyme activity enzyme inactivation enzyme stability heat tolerance physical chemistry storage temperature temperature The objective was to study the remaining activity of the enzyme β-galactosidase in dehydrated dairy systems and its relationship with simultaneous chemical (i.e. non-enzymatic browning, NEB) and physical changes (structural collapse) at temperatures from 70 to 105°C. The presence of milk proteins had a structure-stabilizing effect, which was not reflected by enzymic stabilization or NEB prevention. Although the remaining enzyme activity was correlated with physical and chemical changes in some of the systems exposed at 22% R.H., these changes were not parallel to the macroscopic changes in some of the anhydrous systems. The single lactose systems were highly collapsed at all the temperatures analyzed, but enzymic inactivation and NEB were dependent on the storage temperature rather than on the degree of collapse. Chemical and physical changes were not correlated to the remaining activity. Changes which occur at a molecular level may not be related to the changes at a supramolecular level (such as those derived from glass transition or collapse). © 2002 Elsevier Science Ltd. All rights reserved. Fil:Burin, L. 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. Fil:Hough, G. 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_03088146_v76_n4_p423_Burin
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-galactosidase
Dehydrated dairy products
Enzyme stability
Glass transition
Non enzymatic browning: Collapse
beta galactosidase
lactose
milk protein
article
dairy product
dehydration
enzyme activity
enzyme inactivation
enzyme stability
heat tolerance
physical chemistry
storage temperature
temperature
spellingShingle β-galactosidase
Dehydrated dairy products
Enzyme stability
Glass transition
Non enzymatic browning: Collapse
beta galactosidase
lactose
milk protein
article
dairy product
dehydration
enzyme activity
enzyme inactivation
enzyme stability
heat tolerance
physical chemistry
storage temperature
temperature
Burin, L.
Buera, M.P.
Hough, G.
Chirife, J.
Thermal resistance of β-galactosidase in dehydrated dairy model systems as affected by physical and chemical changes
topic_facet β-galactosidase
Dehydrated dairy products
Enzyme stability
Glass transition
Non enzymatic browning: Collapse
beta galactosidase
lactose
milk protein
article
dairy product
dehydration
enzyme activity
enzyme inactivation
enzyme stability
heat tolerance
physical chemistry
storage temperature
temperature
description The objective was to study the remaining activity of the enzyme β-galactosidase in dehydrated dairy systems and its relationship with simultaneous chemical (i.e. non-enzymatic browning, NEB) and physical changes (structural collapse) at temperatures from 70 to 105°C. The presence of milk proteins had a structure-stabilizing effect, which was not reflected by enzymic stabilization or NEB prevention. Although the remaining enzyme activity was correlated with physical and chemical changes in some of the systems exposed at 22% R.H., these changes were not parallel to the macroscopic changes in some of the anhydrous systems. The single lactose systems were highly collapsed at all the temperatures analyzed, but enzymic inactivation and NEB were dependent on the storage temperature rather than on the degree of collapse. Chemical and physical changes were not correlated to the remaining activity. Changes which occur at a molecular level may not be related to the changes at a supramolecular level (such as those derived from glass transition or collapse). © 2002 Elsevier Science Ltd. All rights reserved.
format JOUR
author Burin, L.
Buera, M.P.
Hough, G.
Chirife, J.
author_facet Burin, L.
Buera, M.P.
Hough, G.
Chirife, J.
author_sort Burin, L.
title Thermal resistance of β-galactosidase in dehydrated dairy model systems as affected by physical and chemical changes
title_short Thermal resistance of β-galactosidase in dehydrated dairy model systems as affected by physical and chemical changes
title_full Thermal resistance of β-galactosidase in dehydrated dairy model systems as affected by physical and chemical changes
title_fullStr Thermal resistance of β-galactosidase in dehydrated dairy model systems as affected by physical and chemical changes
title_full_unstemmed Thermal resistance of β-galactosidase in dehydrated dairy model systems as affected by physical and chemical changes
title_sort thermal resistance of β-galactosidase in dehydrated dairy model systems as affected by physical and chemical changes
url http://hdl.handle.net/20.500.12110/paper_03088146_v76_n4_p423_Burin
work_keys_str_mv AT burinl thermalresistanceofbgalactosidaseindehydrateddairymodelsystemsasaffectedbyphysicalandchemicalchanges
AT bueramp thermalresistanceofbgalactosidaseindehydrateddairymodelsystemsasaffectedbyphysicalandchemicalchanges
AT houghg thermalresistanceofbgalactosidaseindehydrateddairymodelsystemsasaffectedbyphysicalandchemicalchanges
AT chirifej thermalresistanceofbgalactosidaseindehydrateddairymodelsystemsasaffectedbyphysicalandchemicalchanges
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