Analysis of protein structures and interactions in complex food by near-infrared spectroscopy. 2. Hydrated gluten.
Hydrated gluten, treated with various salts, was analyzed by near-infrared (NIR) spectroscopy to assess the ability of this method to reveal protein structure and interaction changes in perturbed food systems. The spectra were pretreated with second-derivative transformation and extended multiplicative signal correction for improving the band resolution and removing physical and quantitative spectral variations. Principal component analysis of the preprocessed spectra showed spectral effects that depended on salt type and concentration. Although both gluten texture and the NIR spectra were little influenced by treatment with salt solutions of low concentrations (0.1-0.2 M), they were significantly and diversely affected by treatment with 1.0 M salt solutions. Compared to hydration in water, hydration in 1.0 M sulfate salts caused spectral effects similar to a drying-out effect, which could be explained by salting-out.
Bruun
Susanne Wrang
SW
Enzyme and Protein Chemistry, BioCentrum-DTU, Søltofts Plads, Building 224, Technical University of Denmark, DK-2800 Kgs. Lyngby, Denmark.
Søndergaard
Ib
I
Jacobsen
Susanne
S
D004044:Dietary Proteins / Q000032:analysis*; D005983:Glutens / Q000737:chemistry*; D012996:Solutions; D019265:Spectroscopy, Near-Infrared; D013431:Sulfates / Q000737:chemistry; D014867:Water / Q000737:chemistry
D004044:Dietary Proteins; D012996:Solutions; D013431:Sulfates; D014867:Water; D005983:Glutens