Monitoring Protein Structural Changes and Hydration in Bovine Meat Tissue Due to Salt Substitutes by Fourier Transform Infrared (FTIR) Microspectroscopy
Open Access
- 10 August 2011
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of Agricultural and Food Chemistry
- Vol. 59 (18), 10052-10061
- https://doi.org/10.1021/jf201578b
Abstract
The objective of this study was to investigate the influence of NaCl and two salt substitutes, MgSO4 and KCl, in different concentrations (1.5, 6.0, and 9.0%) on meat proteins by using Fourier transform infrared (FTIR) microspectroscopy. Hydration properties and secondary structural properties of proteins were investigated by studying the amide I, amide II, and water regions (3500–3000 cm–1) in FTIR spectra. By applying multivariate analysis (PCA and PLSR), differences between samples according to salt concentration and salt type were found and correlated to spectral bands. The most distinctive differences related to salt type were obtained by using the water region. It was found that samples salted with MgSO4 exhibited hydration and subsequent denaturation of proteins at lower concentrations than those salted with NaCl. Samples salted with KCl brines showed less denaturation even at the 9.0% concentration. The FTIR results were further supported by water-binding capacity (WBC) measurements.Keywords
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