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, Viviana M., Pilosof, Ana María Renata
Publicado: 2001
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: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
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
id paper:paper_87567938_v17_n4_p775_Taragano
record_format dspace
spelling 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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