Timed Emulsification Studies with Chicken Breast Muscle: Soluble and Insoluble Myofibrillar Proteins

Emulsion formation with chicken breast muscle was investigated using timed emulsification. High-salt soluble proteins (pH 7.0, 0.6M NaCl) extracted from previously washed muscle (pH 7.0, 0.05M NaCl) were removed from the aqueous phase as mixing time increased. Low- and high-salt exhaustively washed muscle, resuspended in either 0.15 or 0.6M NaCl, pH 7.0, still exhibited good emulsion properties. The pellet protein decreased (> 90%) as mixing time increased from 0 to 5 min. Addition of sodium pyrophosphate to 0.6M NaCl suspensions of 0.05M NaCl washed muscle resulted in an increase in solubility of myofibrillar proteins and a general improvement in emulsification properties. High-salt insoluble proteins may play an important role in emulsion formation.