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Aggregation of egg white proteins with pulsed electric fields and thermal processes
Author(s) -
Wu Li,
Zhao Wei,
Yang Ruijin,
Yan Wenxu,
Sun Qianyan
Publication year - 2016
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.7512
Subject(s) - egg white , electric field , white (mutation) , chemistry , biophysics , biology , food science , biochemistry , physics , quantum mechanics , gene
BACKGROUND Pulsed electric field ( PEF ) processing is progressing towards application for liquid egg to ensure microbial safety. However, it usually causes protein aggregation, and the mechanism is still unclear. In this study, egg white protein was applied to investigate the changes in protein structure and mechanism of aggregates formation and a comparison was made with thermal treatment. RESULTS Soluble protein content decreased with the increase of turbidity after both treatments. Fluorescence intensity and free sulfhydryl content were increased after being treated at 70 °C for 4 min. Less‐remarkable changes of hydrophobicity were observed after PEF treatments (30 kV cm −1 , 800 µs). Soluble and insoluble aggregates were observed by thermal treatment, and disulfide bonds were the main binding forces. The main components of insoluble aggregates formed by thermal treatment were ovotransferrin (30.58%), lysozyme (18.47%) and ovalbumin (14.20%). While only insoluble aggregates were detected during PEF processes, which consists of ovotransferrin (11.86%), lysozyme (21.11%) and ovalbumin (31.07%). Electrostatic interaction played a very important role in the aggregates formation. CONCLUSION PEF had a minor impact on the structure of egg white protein. PEF had insignificant influence on heat‐sensitive protein, indicating that PEF has potential in processing food with high biological activity and heat sensitive properties. © 2015 Society of Chemical Industry