Stability of enzymes and proteins in dried glassy systems: Effect of simulated sunlight conditions

The purpose of the present work was to study the effects of simulated sunlight conditions on enzyme inactivation and structural damage in dehydrated glassy systems. Freeze-dried samples containing different enzymes (lactase, invertase, lysozyme and amyloglucosidase) were exposed to light using a med...

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Autores principales:	Espinosa, L., Schebor, C., Nudelman, N.S., Chirife, J.
Formato:	JOUR
Materias:	Dehydration Electrophoresis Enzyme kinetics Enzymes Freezing Glass Solar energy Dried glassy systems Enzyme inactivation Structural damage Biotechnology enzyme glass protein article chemistry differential scanning calorimetry enzyme stability polyacrylamide gel electrophoresis protein conformation sunlight Calorimetry, Differential Scanning Electrophoresis, Polyacrylamide Gel Enzyme Stability Protein Conformation Proteins Sunlight
Acceso en línea:	http://hdl.handle.net/20.500.12110/paper_87567938_v20_n4_p1220_Espinosa
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	todo:paper_87567938_v20_n4_p1220_Espinosa
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spelling	todo:paper_87567938_v20_n4_p1220_Espinosa2023-10-03T16:42:34Z Stability of enzymes and proteins in dried glassy systems: Effect of simulated sunlight conditions Espinosa, L. Schebor, C. Nudelman, N.S. Chirife, J. Dehydration Electrophoresis Enzyme kinetics Enzymes Freezing Glass Solar energy Dried glassy systems Enzyme inactivation Structural damage Biotechnology enzyme glass protein article chemistry differential scanning calorimetry enzyme stability polyacrylamide gel electrophoresis protein conformation sunlight Calorimetry, Differential Scanning Electrophoresis, Polyacrylamide Gel Enzyme Stability Enzymes Glass Protein Conformation Proteins Sunlight The purpose of the present work was to study the effects of simulated sunlight conditions on enzyme inactivation and structural damage in dehydrated glassy systems. Freeze-dried samples containing different enzymes (lactase, invertase, lysozyme and amyloglucosidase) were exposed to light using a medium-pressure metal halide HPA 400 W lamp. After 1 h of light exposure, the samples showed a significant reduction (more than 50%) in the denaturation peak area as analyzed by DSC, and this could be attributed to protein denaturation. For most of the pure enzymes, the loss of enzymic activity after 1 h of light exposure was around 50%. In the case of enzymes included in anhydrous model systems (trehalose, raffinose, maltodextrin, and dextran), the remaining activity also decreased dramatically during the light treatment. We showed that the light exposure in dehydrated systems generated both the loss of enzymic activity and structural changes such as denaturation (observed by DSC) and protein fragmentation and aggregation (observed by electrophoresis). Overall, we can conclude that a short exposure to the light produces dramatic changes in the enzymic activity in dehydrated systems with or without protective matrices. Fil:Schebor, C. 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_v20_n4_p1220_Espinosa
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	Dehydration Electrophoresis Enzyme kinetics Enzymes Freezing Glass Solar energy Dried glassy systems Enzyme inactivation Structural damage Biotechnology enzyme glass protein article chemistry differential scanning calorimetry enzyme stability polyacrylamide gel electrophoresis protein conformation sunlight Calorimetry, Differential Scanning Electrophoresis, Polyacrylamide Gel Enzyme Stability Enzymes Glass Protein Conformation Proteins Sunlight
spellingShingle	Dehydration Electrophoresis Enzyme kinetics Enzymes Freezing Glass Solar energy Dried glassy systems Enzyme inactivation Structural damage Biotechnology enzyme glass protein article chemistry differential scanning calorimetry enzyme stability polyacrylamide gel electrophoresis protein conformation sunlight Calorimetry, Differential Scanning Electrophoresis, Polyacrylamide Gel Enzyme Stability Enzymes Glass Protein Conformation Proteins Sunlight Espinosa, L. Schebor, C. Nudelman, N.S. Chirife, J. Stability of enzymes and proteins in dried glassy systems: Effect of simulated sunlight conditions
topic_facet	Dehydration Electrophoresis Enzyme kinetics Enzymes Freezing Glass Solar energy Dried glassy systems Enzyme inactivation Structural damage Biotechnology enzyme glass protein article chemistry differential scanning calorimetry enzyme stability polyacrylamide gel electrophoresis protein conformation sunlight Calorimetry, Differential Scanning Electrophoresis, Polyacrylamide Gel Enzyme Stability Enzymes Glass Protein Conformation Proteins Sunlight
description	The purpose of the present work was to study the effects of simulated sunlight conditions on enzyme inactivation and structural damage in dehydrated glassy systems. Freeze-dried samples containing different enzymes (lactase, invertase, lysozyme and amyloglucosidase) were exposed to light using a medium-pressure metal halide HPA 400 W lamp. After 1 h of light exposure, the samples showed a significant reduction (more than 50%) in the denaturation peak area as analyzed by DSC, and this could be attributed to protein denaturation. For most of the pure enzymes, the loss of enzymic activity after 1 h of light exposure was around 50%. In the case of enzymes included in anhydrous model systems (trehalose, raffinose, maltodextrin, and dextran), the remaining activity also decreased dramatically during the light treatment. We showed that the light exposure in dehydrated systems generated both the loss of enzymic activity and structural changes such as denaturation (observed by DSC) and protein fragmentation and aggregation (observed by electrophoresis). Overall, we can conclude that a short exposure to the light produces dramatic changes in the enzymic activity in dehydrated systems with or without protective matrices.
format	JOUR
author	Espinosa, L. Schebor, C. Nudelman, N.S. Chirife, J.
author_facet	Espinosa, L. Schebor, C. Nudelman, N.S. Chirife, J.
author_sort	Espinosa, L.
title	Stability of enzymes and proteins in dried glassy systems: Effect of simulated sunlight conditions
title_short	Stability of enzymes and proteins in dried glassy systems: Effect of simulated sunlight conditions
title_full	Stability of enzymes and proteins in dried glassy systems: Effect of simulated sunlight conditions
title_fullStr	Stability of enzymes and proteins in dried glassy systems: Effect of simulated sunlight conditions
title_full_unstemmed	Stability of enzymes and proteins in dried glassy systems: Effect of simulated sunlight conditions
title_sort	stability of enzymes and proteins in dried glassy systems: effect of simulated sunlight conditions
url	http://hdl.handle.net/20.500.12110/paper_87567938_v20_n4_p1220_Espinosa
work_keys_str_mv	AT espinosal stabilityofenzymesandproteinsindriedglassysystemseffectofsimulatedsunlightconditions AT scheborc stabilityofenzymesandproteinsindriedglassysystemseffectofsimulatedsunlightconditions AT nudelmanns stabilityofenzymesandproteinsindriedglassysystemseffectofsimulatedsunlightconditions AT chirifej stabilityofenzymesandproteinsindriedglassysystemseffectofsimulatedsunlightconditions
_version_	1807321436628451328

Stability of enzymes and proteins in dried glassy systems: Effect of simulated sunlight conditions

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