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Revealing Covariance Structures in Fourier Transform Infrared and Raman Microspectroscopy Spectra: A Study on Pork Muscle Fiber Tissue Subjected to Different Processing Parameters
Volume 61, Number 10 (Oct. 2007) Page 1032-1039
Böcker, Ulrike; Ofstad, Ragni; Wu, Zhiyun; Bertram, Hanne Christine; Sockalingum, Ganesh D.; Manfait, Michel; Egelandsdal, Bjørg; Kohler, Achim
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 1031, 1061, and 1081 cm−1 are related to the IR bands indicative of aggregated β-structures, while the Raman bands at 901 cm−1 and 934 cm−1 showed a strong correlation with IR bands assigned to a α-helical structures. At the same time, the IR band at 1610 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 1610 cm−1 found in pork muscle tissue is not originating from tyrosine.