Trehalose-water-salt interactions related to the stability of β-galactosidase in supercooled media

The conservation of desirable properties in foods and ingredients is often based on the maintenance of the amorphous metastable properties of the systems. Enzymes may be stabilized by drying in saccharide matrices, but a second excipient is generally required to improve sugar protective effects. The...

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Autores principales: Santagapita, Patricio Román, Buera, María del Pilar
Publicado: 2008
Materias:
β-galactosidase
Amorphous systems
Crystallization
Enzyme stability
Freeze-drying
Salts
Trehalose
Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_15571858_v3_n1_p87_Santagapita
http://hdl.handle.net/20.500.12110/paper_15571858_v3_n1_p87_Santagapita
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
id paper:paper_15571858_v3_n1_p87_Santagapita
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spelling paper:paper_15571858_v3_n1_p87_Santagapita2023-06-08T16:23:18Z Trehalose-water-salt interactions related to the stability of β-galactosidase in supercooled media Santagapita, Patricio Román Buera, María del Pilar β-galactosidase Amorphous systems Crystallization Enzyme stability Freeze-drying Salts Trehalose The conservation of desirable properties in foods and ingredients is often based on the maintenance of the amorphous metastable properties of the systems. Enzymes may be stabilized by drying in saccharide matrices, but a second excipient is generally required to improve sugar protective effects. The effect of electrolytes on the thermophysical properties of sugar systems is of special interest because of their major influence on water structure and their possible interactions with biomolecules. Salts affect the kinetics of very important changes in sugar systems such as crystallization. The purpose of the present work was to analyze fungal β-galactosidase stability in supercooled systems of trehalose-containing electrolytes (water soluble acetates, citrates, and chlorides of magnesium and potassium). The degree of sugar crystallization was also related to enzyme stability. Potassium citrate and acetate improved enzyme stability during freeze-drying and thermal treatment of samples at water activity (a w) of 0.22. However, trehalose crystallization inhibition at a w∈=∈0.43 (which was about 50-60%, related to the system without salt) impaired enzyme protection. Certain salts may act retarding sugar crystallization, but in the presence of salts, trehalose crystallization is even more critical because the enzyme is confined in a highly salt-concentrated region. Thus, crystallization inhibition by sugar-salt combinations should be carefully conducted. © 2007 Springer Science+Business Media, LLC. Fil:Santagapita, P.R. 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. 2008 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_15571858_v3_n1_p87_Santagapita http://hdl.handle.net/20.500.12110/paper_15571858_v3_n1_p87_Santagapita
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
Amorphous systems
Crystallization
Enzyme stability
Freeze-drying
Salts
Trehalose
spellingShingle β-galactosidase
Amorphous systems
Crystallization
Enzyme stability
Freeze-drying
Salts
Trehalose
Santagapita, Patricio Román
Buera, María del Pilar
Trehalose-water-salt interactions related to the stability of β-galactosidase in supercooled media
topic_facet β-galactosidase
Amorphous systems
Crystallization
Enzyme stability
Freeze-drying
Salts
Trehalose
description The conservation of desirable properties in foods and ingredients is often based on the maintenance of the amorphous metastable properties of the systems. Enzymes may be stabilized by drying in saccharide matrices, but a second excipient is generally required to improve sugar protective effects. The effect of electrolytes on the thermophysical properties of sugar systems is of special interest because of their major influence on water structure and their possible interactions with biomolecules. Salts affect the kinetics of very important changes in sugar systems such as crystallization. The purpose of the present work was to analyze fungal β-galactosidase stability in supercooled systems of trehalose-containing electrolytes (water soluble acetates, citrates, and chlorides of magnesium and potassium). The degree of sugar crystallization was also related to enzyme stability. Potassium citrate and acetate improved enzyme stability during freeze-drying and thermal treatment of samples at water activity (a w) of 0.22. However, trehalose crystallization inhibition at a w∈=∈0.43 (which was about 50-60%, related to the system without salt) impaired enzyme protection. Certain salts may act retarding sugar crystallization, but in the presence of salts, trehalose crystallization is even more critical because the enzyme is confined in a highly salt-concentrated region. Thus, crystallization inhibition by sugar-salt combinations should be carefully conducted. © 2007 Springer Science+Business Media, LLC.
author Santagapita, Patricio Román
Buera, María del Pilar
author_facet Santagapita, Patricio Román
Buera, María del Pilar
author_sort Santagapita, Patricio Román
title Trehalose-water-salt interactions related to the stability of β-galactosidase in supercooled media
title_short Trehalose-water-salt interactions related to the stability of β-galactosidase in supercooled media
title_full Trehalose-water-salt interactions related to the stability of β-galactosidase in supercooled media
title_fullStr Trehalose-water-salt interactions related to the stability of β-galactosidase in supercooled media
title_full_unstemmed Trehalose-water-salt interactions related to the stability of β-galactosidase in supercooled media
title_sort trehalose-water-salt interactions related to the stability of β-galactosidase in supercooled media
publishDate 2008
url https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_15571858_v3_n1_p87_Santagapita
http://hdl.handle.net/20.500.12110/paper_15571858_v3_n1_p87_Santagapita
work_keys_str_mv AT santagapitapatricioroman trehalosewatersaltinteractionsrelatedtothestabilityofbgalactosidaseinsupercooledmedia
AT bueramariadelpilar trehalosewatersaltinteractionsrelatedtothestabilityofbgalactosidaseinsupercooledmedia
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