MEAT BATTER PROTEINS - EFFECT OF CHEMICAL MODIFICATION ON STRUCTURE

The effects of five chemicals (H2O2, beta-mercaptoethanol, EDTA, urea and Tween 80) on the structure of meat protein extracts from commercia l-type poultry meat batters were studied. Disulphide bonds appeared to affect protein conformation by influencing the interactions in which hydrophobic residues were involved. The spectrophotometric data for ED TA suggested that one of the mechanisms by which it caused meat batter protein aggregation was by salt-bridge formation through sulphydryl r esidues. Urea caused exposure of the hydrophobic residues in the meat batters' proteins. Tween 80 did not appear to directly affect the prot ein-protein interaction.