Acid gelation of mixed thermal aggregates of pea globulins and beta-lactoglobulin
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Titre | Acid gelation of mixed thermal aggregates of pea globulins and beta-lactoglobulin |
Type de publication | Journal Article |
Year of Publication | 2018 |
Auteurs | Chihi M-L, Sok N, Saurel R |
Journal | FOOD HYDROCOLLOIDS |
Volume | 85 |
Pagination | 120-128 |
Date Published | DEC |
Type of Article | Article |
ISSN | 0268-005X |
Mots-clés | Acid gelation, beta-lactoglobulin, Pea globulins, Thermal aggregates |
Résumé | The acid gelation by glucono-delta-lactone of thermal protein aggregates from mixed pea globulin (Glob) and beta-lactoglobulin (beta lg), namely ``mixed-aggregates'', was investigated at 25 degrees C in comparison to that of mixtures of thermal aggregates of each protein obtained beforehand separately (''mixtures of aggregates''). A phase diagram indicating thermal gelation and acid gelation conditions was obtained from mixed protein systems varying in concentration and composition. The minimum acid gelation concentration was 3% regardless of the protein aggregates system, a value about half the concentration threshold measured for thermal gelation. The rheological properties, the microstructure and the water holding capacity (WHC) of acid gels were then evaluated from 4 wt% protein aggregate solutions at different beta lg/Glob weight ratios (0/100, 30/70, 50/50, 70/30 and 100/0). Acid gelation led to weak viscoelastic gels and the gel strength increased with beta lg content. The formation of acid gel from ``mixed-aggregates'' resulted in more elastic gels and improved WHC compared to gels resulting from ``mixtures of aggregates''. This behavior seemed to correlate with the regular filamentous and highly entangled gel network structure observed for mixed-aggregates. These properties were believed to originate from the initial structure of the thermal protein aggregates strongly influenced by beta lg content. |
DOI | 10.1016/j.foodhyd.2018.07.006 |