The effects of chemical modifications by hydrogen peroxide, β-mercaptoethanol, EDTA, urea and polyethylene sorbitan monooleate on raw and cooked meat batters (i.e. with 25% fat) were studied. Eight major proteins were recovered from the meat batters. Correlation of extracted protein concentration with batter stability showed that soluble myosin (in the aqueous phase) correlated best with fat stabilization in the raw batters and water binding during cooking. The results suggest that Z-nin, the major protein present in the aqueous phase, was mainly involved in binding the interfacial protein film around the fat globules to the protein matrix. The reduction of disulphide bonds increased total protein extracted from the meat batters. The results also suggest that disulphide bond formation influenced the amount of myosin and actomyosin present in the aqueous phase.