Pulsed electric fields effects on the molecular structure and gelation of β-lactoglobulin concentrate and egg white

The structure modification of egg white proteins and β-lactoglobulin concentrate when subjected to long length pulses of high intensity electric fields (12.5 kV/cm) was evaluated and related to their sol-gel transition behavior. Both proteins were partially denatured (26-40%) when applying up to 10...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Perez, O.E., Pilosof, A.M.R.
Formato:	JOUR
Materias:	Differential scanning calorimetry Egg white Gelation Pulsed electric fields β-Lactoglobulin Agglomeration Chemical bonds Conformations Electric field effects Electrophoresis Molecular structure Proteins Reaction kinetics Sol-gels Thermodynamic stability Food products
Acceso en línea:	http://hdl.handle.net/20.500.12110/paper_09639969_v37_n1_p102_Perez
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	todo:paper_09639969_v37_n1_p102_Perez
record_format	dspace
spelling	todo:paper_09639969_v37_n1_p102_Perez2023-10-03T15:54:37Z Pulsed electric fields effects on the molecular structure and gelation of β-lactoglobulin concentrate and egg white Perez, O.E. Pilosof, A.M.R. Differential scanning calorimetry Egg white Gelation Pulsed electric fields β-Lactoglobulin Agglomeration Chemical bonds Conformations Electric field effects Electrophoresis Gelation Molecular structure Proteins Reaction kinetics Sol-gels Thermodynamic stability Egg white Food products The structure modification of egg white proteins and β-lactoglobulin concentrate when subjected to long length pulses of high intensity electric fields (12.5 kV/cm) was evaluated and related to their sol-gel transition behavior. Both proteins were partially denatured (26-40%) when applying up to 10 pulses in the order of milliseconds. However, whilst the onset and peak, denaturation temperatures of the β-lactoglobulin concentrate were reduced by approximately 4-5°C, the thermostability of egg white proteins was partially increased. Electrophoresis analysis revealed the formation of aggregates involving covalent bonds. The gelation rate of β-lactoglobulin concentrate was increased after the electric-treatment. In contrast, the gelation rate of egg white at 63°C was lowered. © 2003 Elsevier Ltd. All rights reserved. Fil:Perez, O.E. 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_09639969_v37_n1_p102_Perez
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	Differential scanning calorimetry Egg white Gelation Pulsed electric fields β-Lactoglobulin Agglomeration Chemical bonds Conformations Electric field effects Electrophoresis Gelation Molecular structure Proteins Reaction kinetics Sol-gels Thermodynamic stability Egg white Food products
spellingShingle	Differential scanning calorimetry Egg white Gelation Pulsed electric fields β-Lactoglobulin Agglomeration Chemical bonds Conformations Electric field effects Electrophoresis Gelation Molecular structure Proteins Reaction kinetics Sol-gels Thermodynamic stability Egg white Food products Perez, O.E. Pilosof, A.M.R. Pulsed electric fields effects on the molecular structure and gelation of β-lactoglobulin concentrate and egg white
topic_facet	Differential scanning calorimetry Egg white Gelation Pulsed electric fields β-Lactoglobulin Agglomeration Chemical bonds Conformations Electric field effects Electrophoresis Gelation Molecular structure Proteins Reaction kinetics Sol-gels Thermodynamic stability Egg white Food products
description	The structure modification of egg white proteins and β-lactoglobulin concentrate when subjected to long length pulses of high intensity electric fields (12.5 kV/cm) was evaluated and related to their sol-gel transition behavior. Both proteins were partially denatured (26-40%) when applying up to 10 pulses in the order of milliseconds. However, whilst the onset and peak, denaturation temperatures of the β-lactoglobulin concentrate were reduced by approximately 4-5°C, the thermostability of egg white proteins was partially increased. Electrophoresis analysis revealed the formation of aggregates involving covalent bonds. The gelation rate of β-lactoglobulin concentrate was increased after the electric-treatment. In contrast, the gelation rate of egg white at 63°C was lowered. © 2003 Elsevier Ltd. All rights reserved.
format	JOUR
author	Perez, O.E. Pilosof, A.M.R.
author_facet	Perez, O.E. Pilosof, A.M.R.
author_sort	Perez, O.E.
title	Pulsed electric fields effects on the molecular structure and gelation of β-lactoglobulin concentrate and egg white
title_short	Pulsed electric fields effects on the molecular structure and gelation of β-lactoglobulin concentrate and egg white
title_full	Pulsed electric fields effects on the molecular structure and gelation of β-lactoglobulin concentrate and egg white
title_fullStr	Pulsed electric fields effects on the molecular structure and gelation of β-lactoglobulin concentrate and egg white
title_full_unstemmed	Pulsed electric fields effects on the molecular structure and gelation of β-lactoglobulin concentrate and egg white
title_sort	pulsed electric fields effects on the molecular structure and gelation of β-lactoglobulin concentrate and egg white
url	http://hdl.handle.net/20.500.12110/paper_09639969_v37_n1_p102_Perez
work_keys_str_mv	AT perezoe pulsedelectricfieldseffectsonthemolecularstructureandgelationofblactoglobulinconcentrateandeggwhite AT pilosofamr pulsedelectricfieldseffectsonthemolecularstructureandgelationofblactoglobulinconcentrateandeggwhite
_version_	1807315882471325696

Pulsed electric fields effects on the molecular structure and gelation of β-lactoglobulin concentrate and egg white

Ejemplares similares