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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Autores principales:	Taragano, V.M., Pilosof, A.M.R.
Formato:	JOUR
Materias:	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 Water
Acceso en línea:	http://hdl.handle.net/20.500.12110/paper_87567938_v17_n4_p775_Taragano
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	todo:paper_87567938_v17_n4_p775_Taragano
record_format	dspace
spelling	todo:paper_87567938_v17_n4_p775_Taragano2023-10-03T16:42:34Z Calorimetric studies on dry pectinlyase preparations: Impact of glass transition on inactivation kinetics Taragano, V.M. Pilosof, A.M.R. 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. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar 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, V.M. Pilosof, A.M.R. 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.
format	JOUR
author	Taragano, V.M. Pilosof, A.M.R.
author_facet	Taragano, V.M. Pilosof, A.M.R.
author_sort	Taragano, V.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
url	http://hdl.handle.net/20.500.12110/paper_87567938_v17_n4_p775_Taragano
work_keys_str_mv	AT taraganovm calorimetricstudiesondrypectinlyasepreparationsimpactofglasstransitiononinactivationkinetics AT pilosofamr calorimetricstudiesondrypectinlyasepreparationsimpactofglasstransitiononinactivationkinetics
_version_	1807322843260649472

Calorimetric studies on dry pectinlyase preparations: Impact of glass transition on inactivation kinetics

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