Abstract
Alpha-lactalbumin is an important dairy protein ingredient, and has been widely used in high-protein foods such as infant formula and nutritional bars for its nutritional and functional properties. The purpose of this study was to investigate the moisture-induced aggregation ofalpha-lactalbumin in premixed protein dough model systems, and to illustrate the effects of temperature, cations, and pH on the progress of protein aggregation. Our results suggested that storage temperature was a critical factor for protein aggregation in model systems, and the formation of protein aggregates became faster with increases in storage temperature. Calcium significantly improved the thermal stability ofalpha-lactalbumin and slowed down the formation of protein aggregates. The increases in pH accelerated the aggregation ofalpha-lactalbumin. Our results also suggested that the formation of intermolecular disulfide bonds together with noncovalent interactions are the main mechanisms resulting in the moisture-induced aggregation ofalpha-lactalbumin in model systems.
Original language | English (US) |
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Pages (from-to) | C817-C823 |
Journal | Journal of food science |
Volume | 76 |
Issue number | 6 |
DOIs | |
State | Published - Aug 2011 |
Keywords
- Aggregation
- Alpha-lactalbumin
- Cation
- Disulfide bonding
- Temperature