Myofibrillar proteins (MPs) of chicken breast were generally insoluble in water. The potential of high-pressure homogenization (HPH) to solubilize chicken breast MPs in water was tested. The effects of 0 psi (0.1 MPa), 10,000 psi (69 MPa), 15,000 psi (103 MPa) and 20,000 psi (138 MPa) for two passes HPH on solubility, protein profile, particle property, flow property and microstructure of MPs in water were investigated. HPH at 15,000 psi (103 MPa) could induce the suspension of MPs with small particle size species (sub-filament, oligomers or monomer structure) and high absolute zeta potential, thus enhancing the solubility, flow ability and stability without individual protein degradation. Reduction of particle size and strengthening of intermolecular electrostatic repulsion appeared to be the main reasons in solubilizing MPs in water treated with HPH. Industrial relevance: The qualitative characteristics of meat products are closely related to the solubility of meat proteins. Myofibrillar proteins (MPs), as major part of total muscle proteins, are generally considered to be insoluble in water. The results showed that high-pressure homogenization has potential application for solubilizing MPs in water to develop new meat-based products in the food industry.

Myofibrillar protein; High pressure homogenization; Solubility; Water; Chicken breast muscle

Jiangnan University