Meat batter proteins—Effect of chemical modification on structure

The effects of five chemicals (H 2 O 2 , β‐mercaptoethanol, EDTA, urea and Tween 80) on the structure of meat protein extracts from commercial‐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 EDTA suggested that one of the mechanisms by which it caused meat batter protein aggregation was by salt‐bridge formation through sulphydryl residues. Urea caused exposure of the hydrophobic residues in the meat batters' proteins Tween 80 did not appear to directly affect the protein‐protein interaction.