Physicochemical and functional properties of the muscle protein fraction of .

The physicochemical and functional properties of myofibrillar protein (MP), sarcoplasmic protein (SP), and myostromin (MY) in muscle were evaluated and reported in this study. These fractions are rich in Glu. Three proteins exhibited significantly different morphologies, colors, and particle sizes. The main protein bands of MP, SP, and MY are 15-220 kDa, 26-60 kDa, and 15-245 kDa, respectively. In particular, MP is more hydrophobic. Three proteins exhibited a maximum UV absorption peak at 270 nm, and all amide I secondary structures were shown to be composed of repetitive units (e.g., α-helices and β-sheets). The three proteins demonstrated a predominantly amorphous halo, with T values of 52.22 °C, 59.16 °C, and 58.09 °C. Regarding their properties in water/oil absorption, emulsification, and foaming, MP is the most preferred, followed by SP and MY. In conclusion, muscle proteins are novel and potential functional nutrition ingredients for the food industry.