In purified pork myosin solutions unfolding of α-helices and the formation of β-sheets played an important role in gel formation . FTIR analyses were thus performed on the same six emulsified meat samples as used for histological examination, formulations without and with 1.5% ESM for all three levels of NaCl and of both uncooked and cooked emulsified meat models, in total 12 samples. Due to their high sensitivity to protein secondary structure, the amide I and II bands (1700-1500 cm -1 ) are often used to study protein folding, unfolding, and aggregation. Figure shows the average of the 2. derivative FTIR spectra in this region obtained from both the muscle fibers and the myofibrillar protein matrix of uncooked and cooked samples. The bands at 1658 cm -1 and 1652 cm -1 decreased in magnitude upon heating for all samples, implying a loss of the native α-helical structure of the myofibrillar proteins.