In a previous study of emulsified meat, prepared without starch and spices, the ratio between aggregated β-sheet structures and α-helical structure varied with the type and amount of salt used in the recipe . To find possible structural differences caused by different NaCl and ESM additions, the ratio of the bands in the range 1658-1652 cm -1 and 1628-1622 cm -1 , representing α-helical and aggregated β-sheet structures, respectively, was calculated from FTIR spectra as described above. In this way, it was possible to determine whether there were differences between the samples with respect to the proportion of helical structures versus aggregated protein structures. The average band ratios (1658-1652/1628-1622) of the cooked emulsified meat models are shown in Figure . Pairwise comparison of the band ratios showed that cooked samples added 1.5% ESM had a significant (p<0.05) larger mean ratio (0.98 ± 0.009) than those without ESM (0.97 ± 0.01). The effect of ESM was merely related to a reduced amount of protein aggregation in samples with 1.0 and 1.5% NaCl (Figure ). The reduced CL of samples added ESM having a higher portion of α-helical structures agrees with Choi and Ma who suggested that water hydration strength of β-sheets is weaker than that of α-helices. In the uncooked samples there were no differences between samples without and with 1.5% ESM added. These results indicate that ESM influenced the secondary structure of the salt solubilized myofibrillar proteins forming the matrix structure of the emulsified meat models and that these proteins were less aggregated during heating. This may be due to a higher pH in emulsified meat models added ESM, increasing negative repulsion forces between the negatively charged myofibrillar proteins and thus promoting a heatstabilizing effect on the protein network . This finding is contrasting to a previous study . In that study there was no significant effect on FTIR spectra in the region 1700-1600 cm -1 measured on heated pork meat with pH between 5.4 and 6.5. This discrepancy may be related to differences between the heat-induced denaturation effect on proteins in intact myofibers versus salt-solubilized matrix proteins. PCA (Figure ) revealed that there were some differences between FTIR spectra obtained in muscle fibers and matrix. The mean value of the ratio (1658-1652/1628-1622) was 0.970 ± 0.01 and 0.985 ± 0.005 for fibers and matrix, respectively, indicating that the fibers became more aggregated by heat denaturation than the matrix.