Premium
Moisture‐Induced Aggregation of Alpha ‐Lactalbumin: Effects of Temperature, Cations, and pH
Author(s) -
Liu Dasong,
Zhou Peng,
Liu Xiaoming,
Labuza Theodore P.
Publication year - 2011
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1750-3841.2011.02277.x
Subject(s) - lactalbumin , alpha lactalbumin , chemistry , protein aggregation , whey protein , ingredient , moisture , food science , calcium , intermolecular force , alpha (finance) , biochemistry , molecule , organic chemistry , medicine , construct validity , nursing , patient satisfaction
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 of alpha ‐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 of alpha ‐lactalbumin and slowed down the formation of protein aggregates. The increases in pH accelerated the aggregation of alpha ‐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 of alpha ‐lactalbumin in model systems. Practical Application: 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. Our results suggested low storage temperature, the presence of calcium and low pH condition can make high‐protein food products containing alpha ‐lactalbumin more stable.