Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
606067 | Food Hydrocolloids | 2006 | 4 Pages |
Abstract
In this study, changes in the secondary structure of ovalbumin (OVA) during sodium caprate-induced gel formation were analyzed by FT-IR to help clarify mechanisms of protein gelation. Due to aggregation, there was an increase in intermolecular β-sheet bands and a decrease in α-helix and intramolecular β-sheet content during sodium caprate-induced gel formation. Furthermore, heat treatment of the gel caused a further enhancement in the content of intermolecular β-sheet bands. These results suggest that, similar to β-lactoglobulin gels, sodium caprate-induced OVA gels and heat-induced OVA gels form by similar mechanisms, although the sodium caprate-induced gel formation is accompanied by less marked changes in protein conformation.
Related Topics
Physical Sciences and Engineering
Chemical Engineering
Colloid and Surface Chemistry
Authors
Naoko Yuno-Ohta,