In order to confirm the effect of ESM on the water distribution, low-field NMR T2 relaxation times were measured on uncooked (Figure , left) and cooked (Figure , right) emulsified meat models. The NMR signal decay could be fitted into two or three separate peaks. In uncooked samples, the two water populations were centered around 1-10 ms (T2B) and around 30-200 ms (T21), and in cooked samples, the three water populations were centered around 1-8 ms (T2B), 10-300 ms (T21) and 250-1300 ms (T22). For gel systems these T2 populations have been assigned to bound water (T2B) associated with macromolecules, immobilized water (T21) located within highly organized protein structures and unbound or free water (T22), respectively . When heated to 70 °C, the T21 relaxation time shifted to lower values and the distribution became broader (Figure , right). The shorter T21 relaxation time reflects a smaller size of the internal structures due to denaturation and aggregation of myofibrillar proteins entrapping water, in addition to a general limited water mobility in the gel system formed during heating . A broader relaxation T21 top reflects inhomogeneity in the gel microstructure and/or different physical environment causing a greater variation in the environment of the water protons . Broadening of the T21 top (Figure , right) is thus in accordance with the difference in microstructure among the sausage samples shown in Figure . PCA was used to reveal differences in the relaxation decay among the samples. Due to significant differences in the T2 relaxation time distribution between uncooked and cooked samples, PCA were performed on uncooked and cooked samples separately. The score plot in Figure (left) of the uncooked samples revealed that the first PC, explaining 86.2% of the variations, is mainly related to the effect of ESM. The corresponding loading plot of PC1 (Figure , right) shows that increased ESM addition reduces the T2 relaxation time indicating that the water is increasingly immobilized. Since T21 is the largest peak most of the variation is due to changes in this peak. A shorter T21 relaxation time reflects a smaller size of the intrinsic structures in which both myofibrillar and added water is entrapped . The influence of NaCl was reflected in the second PC, explaining 13.2 % of the variation in the T2 relaxation times (Figure , left). The variation is mainly due to the differences between samples with 0.5% NaCl and those with 1.0% and 1.5% NaCl. The loading plot of PC2 (Figure , right) shows that the higher salt concentrations result in narrower water peaks, indicating that the water was more homogeneously distributed in the protein structure . The lower T21 relaxation time and the narrower peak in sausages with 1.5% ESM and 1.5% NaCl agreed with the finer and more homogeneous microstructure in these samples (Figure ). Smaller pores and a more homogeneous myofibrillar network structure inhibit the movement of water molecules which thus exchange the spin energy with surrounding water molecules faster . The score plot of the cooked samples is shown in Figure (left). PC1 explains 97.0% of the variation which is mainly affected by the NaCl concentration. The loading plot of PC1 (Figure , right) revealed that the relaxation time increased with higher NaCl concentrations. PC2, explaining 2.7% of the variations is related to narrowing of the T21 peak. Relaxation times measured at the peak of the T21 water population (T21max) were 42 ms, 42 ms and 54 ms for 0.5%, 1.0% and 1.5% NaCl, respectively. Samples with 1.5% ESM had slightly higher T21max than samples with the same salt level without ESM, 44 ms, 47 ms and 62 ms at 0.5%, 1.0% and 1.5% NaCl, respectively. The effect of ESM was most pronounced in samples with 1.5% NaCl and 1.5% ESM. These finding are in accordance with the more homogeneous and less aggregated microstructure of cooked emulsified meat models with increased salt content and ESM as shown in Figure . The T21 relaxation time reflects to which extent that water molecules interact with the highly organized protein structures in the myofibrillar matrix. The increased T21 relaxation time in the cooked samples with ESM may indicate an effect of ESM also on the heat induced gel-formation of the salt solubilized myofibrillar proteins. Previously, it has been shown that both addition of 1% gelatin and 0.2% dermatan sulphate had some effect on the water holding capacity of meat products . ESM contains about 10% collagen and about 0.2% glycosaminoglycans . Since ESM makes up only a small proportion (~ 10%) of the total protein in the sausages, it is therefore unlikely that these components have affected the observed T2 relaxation times.