Alkaline pH-dependent thermal aggregation of chicken breast myosin: formation of soluble aggregates.

Soluble aggregates, instead of insoluble gel network, were formed on heat-treated chicken breast myosin through alkaline pH-induced electrostatic regulation. Heat treatment of myosin at pH 9.0 significantly increased solubility, decreased turbidity, and resulted in the highest content at 260 nm particle size compared with those at pH 7.0 and 8.0. Results indicated that soluble myosin aggregates were produced at pH 9.0. The surface hydrophobicity and reactive sulfhydryl (R-SH) of unheated sample revealed gradual increases with increased pH. This increase was related to the decreased α-helical, thereby suggesting myosin unfolding. After heating, treatment at pH 9.0 showed the lowest surface hydrophobicity and R-SH, which may contribute to the highest dispersibility. Moreover, heated myosin (pH 9.0) after reshifting pH still exhibited excellent stability, which indicated the irreversible soluble aggregates formation. The controlled production of aggregates may provide the possibility of using soluble aggregates as ingredients for expanded meat protein application in beverage products. [ABSTRACT FROM AUTHOR]