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...
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_09639969_v37_n1_p102_Perez http://hdl.handle.net/20.500.12110/paper_09639969_v37_n1_p102_Perez |
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paper:paper_09639969_v37_n1_p102_Perez2023-06-08T15:58:22Z Pulsed electric fields effects on the molecular structure and gelation of β-lactoglobulin concentrate and egg white Pérez, Oscar E. Pilosof, Ana María Renata 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. 2004 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_09639969_v37_n1_p102_Perez 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 Pérez, Oscar E. Pilosof, Ana María Renata 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. |
| author |
Pérez, Oscar E. Pilosof, Ana María Renata |
| author_facet |
Pérez, Oscar E. Pilosof, Ana María Renata |
| author_sort |
Pérez, Oscar 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 |
| publishDate |
2004 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_09639969_v37_n1_p102_Perez http://hdl.handle.net/20.500.12110/paper_09639969_v37_n1_p102_Perez |
| work_keys_str_mv |
AT perezoscare pulsedelectricfieldseffectsonthemolecularstructureandgelationofblactoglobulinconcentrateandeggwhite AT pilosofanamariarenata pulsedelectricfieldseffectsonthemolecularstructureandgelationofblactoglobulinconcentrateandeggwhite |
| _version_ |
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