利用傅里叶变换红外（FTIR）显微光谱监测由于盐替代品导致的牛肉组织中蛋白质结构变化和水合作用。
Monitoring protein structural changes and hydration in bovine meat tissue due to salt substitutes by Fourier transform infrared (FTIR) microspectroscopy.
机构信息
Nofima AS, Osloveien 1, 1430 Ås, Norway.
出版信息
J Agric Food Chem. 2011 Sep 28;59(18):10052-61. doi: 10.1021/jf201578b. Epub 2011 Aug 23.
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.
本研究旨在通过傅里叶变换红外（FTIR）微光谱法研究不同浓度（1.5%、6.0%和 9.0%）的 NaCl 和两种盐替代品（MgSO4 和 KCl）对肉蛋白的影响。通过研究酰胺 I、酰胺 II 和水区域（3500-3000cm-1）的 FTIR 光谱，研究了蛋白质的水合性质和二级结构性质。通过应用多元分析（PCA 和 PLSR），根据盐浓度和盐类型发现了样品之间的差异，并与光谱带相关。通过使用水区域，获得了与盐类型最相关的最显著差异。结果发现，用 MgSO4 腌制的样品在较低浓度下表现出蛋白质的水合和随后的变性，而用 NaCl 腌制的样品则较低。即使在 9.0%的浓度下，用 KCl 盐水腌制的样品变性也较少。FTIR 结果进一步得到水结合能力（WBC）测量的支持。
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