DSC confirmation that vitrification is not necessary for stabilization of the restriction enzyme EcoRI dried with saccharides

The glass transition temperature (T(g)) of preparations of the restriction enzyme EcoRI, vacuum-dried in the presence of sucrose, trehalose, or raffinose, was determined using differential scanning calorimetry. T(g) values were well below those expected for low-moisture sucrose, trehalose, or raffin...

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Autores principales: Buera, María del Pilar, Rossi, Silvia Graciela, Moreno de Colonna, Silvia
Publicado: 1999
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Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_87567938_v15_n3_p577_Buera
http://hdl.handle.net/20.500.12110/paper_87567938_v15_n3_p577_Buera
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spelling paper:paper_87567938_v15_n3_p577_Buera2025-07-30T19:12:36Z DSC confirmation that vitrification is not necessary for stabilization of the restriction enzyme EcoRI dried with saccharides Buera, María del Pilar Rossi, Silvia Graciela Moreno de Colonna, Silvia enzyme stability restriction endonuclease ecori vitrification Drying Enzyme kinetics Glass transition Moisture Plasticizers Polysaccharides Sugar (sucrose) Temperature measurement Vacuum applications Vitrification Low moisture saccharide systems Raffinose Restriction enzyme Trehalose Differential scanning calorimetry The glass transition temperature (T(g)) of preparations of the restriction enzyme EcoRI, vacuum-dried in the presence of sucrose, trehalose, or raffinose, was determined using differential scanning calorimetry. T(g) values were well below those expected for low-moisture sucrose, trehalose, or raffinose, and this was attributed to the presence of glycerol (a plasticizer), which was a main component of the restriction enzyme preparation. This was verified by determining the glass transition temperature of glycerol, which was found to be (onset value) -77 °C. Present results confirmed that vitrification (i.e., glass formation) was not necessary for enzyme protection in present low-moisture saccharide systems. As shown in previous work, enzyme EcoRI was very stable stored at 37/45 °C in spite of the fact that sugar matrices were completely rubbery, as unequivocally demonstrated in the present work. The glass transition temperature (Tg) of preparations of the restriction enzyme EcoRI, vacuum-dried in the presence of sucrose, trehalose, or raffinose, was determined using differential scanning calorimetry. Tg values were well below those expected for low-moisture sucrose, trehalose, or raffinose, and this was attributed to the presence of glycerol (a plasticizer), which was a main component of the restriction enzyme preparation. This was verified by determining the glass transition temperature of glycerol, which was found to be (onset value) -77°C. Present results confirmed that vitrification (i.e., glass formation) was not necessary for enzyme protection in present low-moisture saccharide systems. As shown in previous work, enzyme EcoRI was very stable stored at 37/45°C in spite of the fact that sugar matrices were completely rubbery, as unequivocally demonstrated in the present work. Fil:Buera, M.P. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Rossi, S. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Moreno, S. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 1999 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_87567938_v15_n3_p577_Buera http://hdl.handle.net/20.500.12110/paper_87567938_v15_n3_p577_Buera
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic enzyme stability
restriction endonuclease ecori
vitrification
Drying
Enzyme kinetics
Glass transition
Moisture
Plasticizers
Polysaccharides
Sugar (sucrose)
Temperature measurement
Vacuum applications
Vitrification
Low moisture saccharide systems
Raffinose
Restriction enzyme
Trehalose
Differential scanning calorimetry
spellingShingle enzyme stability
restriction endonuclease ecori
vitrification
Drying
Enzyme kinetics
Glass transition
Moisture
Plasticizers
Polysaccharides
Sugar (sucrose)
Temperature measurement
Vacuum applications
Vitrification
Low moisture saccharide systems
Raffinose
Restriction enzyme
Trehalose
Differential scanning calorimetry
Buera, María del Pilar
Rossi, Silvia Graciela
Moreno de Colonna, Silvia
DSC confirmation that vitrification is not necessary for stabilization of the restriction enzyme EcoRI dried with saccharides
topic_facet enzyme stability
restriction endonuclease ecori
vitrification
Drying
Enzyme kinetics
Glass transition
Moisture
Plasticizers
Polysaccharides
Sugar (sucrose)
Temperature measurement
Vacuum applications
Vitrification
Low moisture saccharide systems
Raffinose
Restriction enzyme
Trehalose
Differential scanning calorimetry
description The glass transition temperature (T(g)) of preparations of the restriction enzyme EcoRI, vacuum-dried in the presence of sucrose, trehalose, or raffinose, was determined using differential scanning calorimetry. T(g) values were well below those expected for low-moisture sucrose, trehalose, or raffinose, and this was attributed to the presence of glycerol (a plasticizer), which was a main component of the restriction enzyme preparation. This was verified by determining the glass transition temperature of glycerol, which was found to be (onset value) -77 °C. Present results confirmed that vitrification (i.e., glass formation) was not necessary for enzyme protection in present low-moisture saccharide systems. As shown in previous work, enzyme EcoRI was very stable stored at 37/45 °C in spite of the fact that sugar matrices were completely rubbery, as unequivocally demonstrated in the present work. The glass transition temperature (Tg) of preparations of the restriction enzyme EcoRI, vacuum-dried in the presence of sucrose, trehalose, or raffinose, was determined using differential scanning calorimetry. Tg values were well below those expected for low-moisture sucrose, trehalose, or raffinose, and this was attributed to the presence of glycerol (a plasticizer), which was a main component of the restriction enzyme preparation. This was verified by determining the glass transition temperature of glycerol, which was found to be (onset value) -77°C. Present results confirmed that vitrification (i.e., glass formation) was not necessary for enzyme protection in present low-moisture saccharide systems. As shown in previous work, enzyme EcoRI was very stable stored at 37/45°C in spite of the fact that sugar matrices were completely rubbery, as unequivocally demonstrated in the present work.
author Buera, María del Pilar
Rossi, Silvia Graciela
Moreno de Colonna, Silvia
author_facet Buera, María del Pilar
Rossi, Silvia Graciela
Moreno de Colonna, Silvia
author_sort Buera, María del Pilar
title DSC confirmation that vitrification is not necessary for stabilization of the restriction enzyme EcoRI dried with saccharides
title_short DSC confirmation that vitrification is not necessary for stabilization of the restriction enzyme EcoRI dried with saccharides
title_full DSC confirmation that vitrification is not necessary for stabilization of the restriction enzyme EcoRI dried with saccharides
title_fullStr DSC confirmation that vitrification is not necessary for stabilization of the restriction enzyme EcoRI dried with saccharides
title_full_unstemmed DSC confirmation that vitrification is not necessary for stabilization of the restriction enzyme EcoRI dried with saccharides
title_sort dsc confirmation that vitrification is not necessary for stabilization of the restriction enzyme ecori dried with saccharides
publishDate 1999
url https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_87567938_v15_n3_p577_Buera
http://hdl.handle.net/20.500.12110/paper_87567938_v15_n3_p577_Buera
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AT rossisilviagraciela dscconfirmationthatvitrificationisnotnecessaryforstabilizationoftherestrictionenzymeecoridriedwithsaccharides
AT morenodecolonnasilvia dscconfirmationthatvitrificationisnotnecessaryforstabilizationoftherestrictionenzymeecoridriedwithsaccharides
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