Effects of High Pressure Homogenization on Physicochemical Properties and Protein Structure of Myofibrillar Protein Aqueous Suspensions with Different Concentrations

Chicken myofibrillar proteins(MPs)were used to study the effects of high pressure homogenization(HPH)on the physicochemical properties and protein structure of MP water suspension with different concentrations(5,10,15 mg/mL)under 103 MPa pressure.The results showed that,HPH could significantly improve the solubility of MP in water at different concentrations(P<0.05),improve the dispersion and rheological properties of MP water suspension,and destroy the protein structure. With the increase of MP concentration,the solubility and stability of MP water suspension decreased(P<0.05). Protein aggregation might occur during HPH treatment of high concentration MP,which resulted in the increase of protein particle size,the increase of apparent viscosity and the decrease of fluidity in water suspension. The secondary and tertiary structure of MP water suspension changed,the surface hydrophobicity decreased,the content of sulfhydryl group increased,the α-helix increased and the β-folding decreased,which affected the solubility of MP water suspension. The solubility of MP water suspension of 5 mg/mL was better after HPH treatment,which reached 88.39%. The solubility of MP water suspension was still 79.08% after 9 d at 4 ℃. This study provided a reference for the further processing of meat protein in food industry.