Calorimetric studies on dry pectinlyase preparations: Impact of glass transition on inactivation kinetics
The glass transition temperature (Tg) of a dry ultrafiltrated pectinlyase (PL) preparation decreased from 56 to 24 °C when water content increased to 20%. The thermal transition temperature (Tp) for protein denaturation decreased greatly up to 40% moisture; above 40% no further changes in Tp were ob...
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2001
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Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_87567938_v17_n4_p775_Taragano http://hdl.handle.net/20.500.12110/paper_87567938_v17_n4_p775_Taragano |
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paper:paper_87567938_v17_n4_p775_Taragano2023-06-08T16:36:54Z Calorimetric studies on dry pectinlyase preparations: Impact of glass transition on inactivation kinetics Taragano, Viviana M. Pilosof, Ana María Renata Dry pectinlyases calorimetry day length electrophoretic mobility enzyme activity enzyme inactivation glass transition temperature pectinlyase Glass transition Moisture Proteins Ultrafiltration Biotechnology Calorimetry, Differential Scanning Enzyme Activation Enzyme Stability Glass Kinetics Polysaccharide-Lyases Ultrafiltration Water The glass transition temperature (Tg) of a dry ultrafiltrated pectinlyase (PL) preparation decreased from 56 to 24 °C when water content increased to 20%. The thermal transition temperature (Tp) for protein denaturation decreased greatly up to 40% moisture; above 40% no further changes in Tp were observed. In the glassy state, a lag period of approximately 7 days with no PL activity loss was observed; after that, PL activity was lost. Above Tg, the rates of PL inactivation greatly increased. In the glassy state Ea was 16.6 kJ/mol. When the system was in a higher mobility state (rubbery), Ea increased to 66.5 kJ/mol. Fil:Taragano, V.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Pilosof, A.M.R. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2001 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_87567938_v17_n4_p775_Taragano http://hdl.handle.net/20.500.12110/paper_87567938_v17_n4_p775_Taragano |
institution |
Universidad de Buenos Aires |
institution_str |
I-28 |
repository_str |
R-134 |
collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
topic |
Dry pectinlyases calorimetry day length electrophoretic mobility enzyme activity enzyme inactivation glass transition temperature pectinlyase Glass transition Moisture Proteins Ultrafiltration Biotechnology Calorimetry, Differential Scanning Enzyme Activation Enzyme Stability Glass Kinetics Polysaccharide-Lyases Ultrafiltration Water |
spellingShingle |
Dry pectinlyases calorimetry day length electrophoretic mobility enzyme activity enzyme inactivation glass transition temperature pectinlyase Glass transition Moisture Proteins Ultrafiltration Biotechnology Calorimetry, Differential Scanning Enzyme Activation Enzyme Stability Glass Kinetics Polysaccharide-Lyases Ultrafiltration Water Taragano, Viviana M. Pilosof, Ana María Renata Calorimetric studies on dry pectinlyase preparations: Impact of glass transition on inactivation kinetics |
topic_facet |
Dry pectinlyases calorimetry day length electrophoretic mobility enzyme activity enzyme inactivation glass transition temperature pectinlyase Glass transition Moisture Proteins Ultrafiltration Biotechnology Calorimetry, Differential Scanning Enzyme Activation Enzyme Stability Glass Kinetics Polysaccharide-Lyases Ultrafiltration Water |
description |
The glass transition temperature (Tg) of a dry ultrafiltrated pectinlyase (PL) preparation decreased from 56 to 24 °C when water content increased to 20%. The thermal transition temperature (Tp) for protein denaturation decreased greatly up to 40% moisture; above 40% no further changes in Tp were observed. In the glassy state, a lag period of approximately 7 days with no PL activity loss was observed; after that, PL activity was lost. Above Tg, the rates of PL inactivation greatly increased. In the glassy state Ea was 16.6 kJ/mol. When the system was in a higher mobility state (rubbery), Ea increased to 66.5 kJ/mol. |
author |
Taragano, Viviana M. Pilosof, Ana María Renata |
author_facet |
Taragano, Viviana M. Pilosof, Ana María Renata |
author_sort |
Taragano, Viviana M. |
title |
Calorimetric studies on dry pectinlyase preparations: Impact of glass transition on inactivation kinetics |
title_short |
Calorimetric studies on dry pectinlyase preparations: Impact of glass transition on inactivation kinetics |
title_full |
Calorimetric studies on dry pectinlyase preparations: Impact of glass transition on inactivation kinetics |
title_fullStr |
Calorimetric studies on dry pectinlyase preparations: Impact of glass transition on inactivation kinetics |
title_full_unstemmed |
Calorimetric studies on dry pectinlyase preparations: Impact of glass transition on inactivation kinetics |
title_sort |
calorimetric studies on dry pectinlyase preparations: impact of glass transition on inactivation kinetics |
publishDate |
2001 |
url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_87567938_v17_n4_p775_Taragano http://hdl.handle.net/20.500.12110/paper_87567938_v17_n4_p775_Taragano |
work_keys_str_mv |
AT taraganovivianam calorimetricstudiesondrypectinlyasepreparationsimpactofglasstransitiononinactivationkinetics AT pilosofanamariarenata calorimetricstudiesondrypectinlyasepreparationsimpactofglasstransitiononinactivationkinetics |
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1768544798573068288 |