Analysis of protein structures and interactions in complex food by near-infrared spectroscopy. 1. Gluten powder.
The potential of near-infrared (NIR) spectroscopy in detailed food analysis was tested in a model system consisting of gluten powder treated with moisture and heat. Second-derivative transformation and extended multiplicative signal correction were applied for improving the band resolution and removing physical and quantitative spectral variations. Subsequent chemometric analyses gave loading spectra, which were interpreted as spectral effects of altered protein structures, induced by the treatments. Moistening of the gluten powder resulted in shifts and intensity changes in the protein bands, which could be explained by a combination of minor secondary structure changes, water binding, and changed microenvironments of the amino acid side chains. Heat denaturation induced increases at 2209 nm and decreases at 2167-2182 nm, indicating an alpha-helix to beta-sheet transformation, in agreement with the expectations.
Enzyme and Protein Chemistry, BioCentrum-DTU, Søltofts Plads, Building 224, Technical University of Denmark, DK-2800 Kgs. Lyngby, Denmark.
Susanne Wrang
SW
Bruun
Ib
I
Søndergaard
Susanne
S
Jacobsen
D004044:Dietary Proteins / Q000032:analysis*; D005519:Food Preservation; D005983:Glutens / Q000737:chemistry*; D006358:Hot Temperature; D011489:Protein Denaturation; D019265:Spectroscopy, Near-Infrared; D014867:Water
D004044:Dietary Proteins; D014867:Water; D005983:Glutens