The aim of this study was to investigate the correlation patterns between Fourier transform infrared (FT-IR) and Raman microspectroscopic data obtained from pork muscle tissue, which helped to improve the interpretation and band assignment of the observed spectral features. The pork muscle tissue was subjected to different processing factors, including aging, salting, and heat treatment, in order to induce the necessary degree of variation of the spectra. For comparing the information gained from the two spectroscopic techniques with respect to the experimental design, multiblock principal component analysis (MPCA) was utilized for data analysis. The results showed that both FT-IR and Raman spectra were mostly affected by heat treatment, followed by the variation in salt content. Furthermore, it could be observed that IR amide I, II, and III band components appear to be effected to a different degree by brine-salting and heating. FT-IR bands assigned to specific protein secondary structures could be related to different Raman C-C stretching bands. The Raman C-C skeletal stretching bands at 1,031, 1,061, and 1,081 cm(-1) are related to the IR bands indicative of aggregated beta-structures, while the Raman bands at 901 cm(-1) and 934 cm(-1) showed a strong correlation with IR bands assigned to a alpha-helical structures. At the same time, the IR band at 1,610 cm(-1), which formerly was assigned to tyrosine in spectra originating from pork muscle, did not show a correlation to the strong tyrosine doublet at 827 and 852 cm(-1) found in Raman spectra, leading to the conclusion that the IR band at 1,610 cm(-1) found in pork muscle tissue is not originating from tyrosine.

Fourier transform infrared (FT-IR) microspectroscopy and low-field (LF) proton NMR transverse relaxation measurements were used to study the changes in protein secondary structure and water distribution as a consequence of aging (1 day and 14 days) followed by salting (3%, 6%, and 9% NaCl) and cooking (65 degrees C). An enhanced water uptake and increased proton NMR relaxation times after salting were observed in aged meat (14 days) compared with nonaged meat (1 day). FT-IR bands revealed that salting induced an increase in native beta-sheet structure while aging triggered an increase in native alpha-helical structure before cooking, which could explain the effects of aging and salting on water distribution and water uptake. Moreover, the decrease in T2 relaxation times and loss of water upon cooking were attributed to an increase in aggregated beta-sheet structures and a simultaneous decrease in native protein structures. Finally, aging increased the cooking loss and subsequently decreased the final yield, which corresponded to a further decrease in T2 relaxation times in aged meat upon cooking. However, salting weakened the effect of aging on the final yield, which is consistent with the increased T2 relaxation times upon salting for aged meat after cooking and the weaker effect of aging on protein secondary structural changes for samples treated with high salt concentration. The present study reveals that changes in water distribution during aging, salting, and cooking are not only due to the accepted causal connection, i.e., proteolytic degradation of myofibrillar structures, change in electrostatic repulsion, and dissolution and denaturation of proteins, but also dynamic changes in specific protein secondary structures.

Water characteristics and meat microstructure of NaHCO3-enhanced pork were compared with NaCl- and Na4O7P2-enhanced pork using low-field proton NMR relaxometry, advanced microscopy techniques, and traditional meat quality measurements. Porcine samples were enhanced at 4 degrees C for 48 h with sodium salts individually and in the following combinations: (i) 5% NaCl, (ii) 5% Na4O7P2, (iii) 3% NaHCO3, (iv) 5% NaCl and 5% Na4O7P2, (v) 5% NaCl and 3% NaHCO3, (vi) 5% Na4O7P2 and 3% NaHCO3, and (vii) 5% NaCl, 5% Na4O7P2, and 3% NaHCO3. Independently of the marinade used, the water-binding capacity was improved, cooking loss was reduced, and the yield was enhanced compared with nonmarinated pork samples. This was also reflected in the water mobility within the samples measured by proton NMR relaxometry. Visualization of samples by confocal laser scanning microscopy (CLSM) revealed salt-dependent microstructural changes in the green pork samples treated with NaHCO3, giving rise to nearly complete disintegration of overall structures. High-resolution visualization by atomic force microscopy (AFM) further suggested that a higher cooking loss in sodium chloride-enhanced samples could be ascribed to less solubilization and higher heat-induced protein denaturation compared with phosphate- and bicarbonate-enhanced samples.

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