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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todo:paper_87567938_v15_n3_p577_Buera2023-10-03T16:42:33Z DSC confirmation that vitrification is not necessary for stabilization of the restriction enzyme EcoRI dried with saccharides Buera, M.P. Rossi, S. Moreno, S. Chirife, J. 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. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar 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, M.P. Rossi, S. Moreno, S. Chirife, J. 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. |
| format |
JOUR |
| author |
Buera, M.P. Rossi, S. Moreno, S. Chirife, J. |
| author_facet |
Buera, M.P. Rossi, S. Moreno, S. Chirife, J. |
| author_sort |
Buera, M.P. |
| 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 |
| url |
http://hdl.handle.net/20.500.12110/paper_87567938_v15_n3_p577_Buera |
| work_keys_str_mv |
AT bueramp dscconfirmationthatvitrificationisnotnecessaryforstabilizationoftherestrictionenzymeecoridriedwithsaccharides AT rossis dscconfirmationthatvitrificationisnotnecessaryforstabilizationoftherestrictionenzymeecoridriedwithsaccharides AT morenos dscconfirmationthatvitrificationisnotnecessaryforstabilizationoftherestrictionenzymeecoridriedwithsaccharides AT chirifej dscconfirmationthatvitrificationisnotnecessaryforstabilizationoftherestrictionenzymeecoridriedwithsaccharides |
| _version_ |
1807315422436917248 |