Journal
JOURNAL OF MOLECULAR STRUCTURE
Volume 1033, Issue -, Pages 51-58Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.molstruc.2012.08.031
Keywords
Raman Spectroscopy; Secondary protein structure; Gluten proteins; Emulsifiers
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Funding
- UNLP
- CONICET
- FONCYT-MINCYT (Argentina)
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Changes in the secondary structure of gluten proteins due to emulsifiers were analyzed by Raman Spectroscopy. The protein folding induced by 0.25% SSL (Sodium Stearoyl Lactylate) (GS0.25, Gluten + 0.25% SSL) included an increase in alpha-helix conformation and a decrease in beta-sheet, turns and random coil. The same behavior, although in a less degree, was observed for 0.5% gluten-DATEM (Diacetyl Tartaric Acid Esters of Monoglycerides) system. The low burial of Tryptophan residues to a more hydrophobic environment and the low percentage area of the C-H stretching band for GS0.25 (Gluten + 0.25% SSL), could be related to the increased in alpha-helix conformation. This behavior was also confirmed by changes in stretching vibrational modes of disulfide bridges (S-S) and the low exposure of Tyrosine residues. High levels of SSL (0.5% and 1.0%) and DATEM (1.0%) led to more disordered protein structures, with different gluten networks. SSL (1.0%) formed a more disordered and opened gluten matrix than DATEM, the last one being laminar and homogeneous. (C) 2012 Elsevier B.V. All rights reserved.
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