Changes in secondary structure of gluten proteins due to emulsifiers

GÓMEZ, A.V.; FERRER, E.G.; AÑÓN, M. C.; PUPPO, M. C.

JOURNAL OF MOLECULAR STRUCTURE

ELSEVIER SCIENCE BV

Lugar: Amsterdam; Año: 2013 vol. 1033 p. 51 - 58

0022-2860

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 α-helix conformation and a decrease in β-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 α-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.