AI Article Synopsis
- The study combined NIR spectroscopy with FTIR and Raman microspectroscopy to investigate how different salts (NaCl, KCl, MgSO(4)) affect muscle protein structure and hydration.
- Multivariate analysis helped integrate data from these techniques, linking macroscopic findings from NIR to microscopic details from FTIR and Raman.
- The results showed that salt concentration influenced protein structure and hydration affinity, with cation-π interactions affecting aromatic amino acid residues' structures significantly.
Article Abstract
In this paper a combination of NIR spectroscopy and FTIR and Raman microspectroscopy was used to elucidate the effects of different salts (NaCl, KCl and MgSO(4)) on structural proteins and their hydration in muscle tissue. Multivariate multi-block technique Consensus Principal Component Analysis enabled integration of different vibrational spectroscopic techniques: macroscopic information obtained by NIR spectroscopy is directly related to microscopic information obtained by FTIR and Raman microspectroscopy. Changes in protein secondary structure observed at different concentrations of salts were linked to changes in protein hydration affinity. The evidence for this was given by connecting the underlying FTIR bands of the amide I region (1700-1600 cm(-1)) and the water region (3500-3000 cm(-1)) with water vibrations obtained by NIR spectroscopy. In addition, Raman microspectroscopy demonstrated that different cations affected structures of aromatic amino acid residues differently, which indicates that cation-π interactions play an important role in determination of the final structure of protein molecules.
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| http://dx.doi.org/10.1016/j.foodchem.2012.10.117 | DOI Listing |
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