INVESTIGADORES
AÑON Maria Cristina
artículos
Título:
Changes in secondary structure of gluten proteins due to emulsifiers
Autor/es:
GÓMEZ, A.V; FERRER, E.G; AÑÓN, M.C; PUPPO, M.C
Revista:
JOURNAL OF MOLECULAR STRUCTURE THEOCHEM
Editorial:
ELSEVIER SCIENCE BV
Referencias:
Lugar: Amsterdam; Año: 2013 vol. 1033 p. 51 - 58
ISSN:
0166-1280
Resumen:
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 a-helix conformation and a decrease in b-sheet, turns and random coil.
The same behavior, although in a less degree, was observed for 0.5% glutenDATEM (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 CH stretching band for GS0.25 (Gluten + 0.25% SSL),
could be related to the increased in a-helix conformation. This behavior was also confirmed by changes
in stretching vibrational modes of disulfide bridges (SS) 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