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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| Autores principales: | , |
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| Formato: | JOUR |
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| Acceso en línea: | http://hdl.handle.net/20.500.12110/paper_09639969_v37_n1_p102_Perez |
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| Sumario: | 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. |
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