title: Disaggregation and reaggregation of gluten proteins by sodium chloride.
abstract: This study showed that gluten proteins were extracted with distilled water from dough prepared in the presence of NaCl. To elucidate the interrelationship of NaCl and gluten proteins in dough, the extracted proteins were characterized. These proteins were primarily found to be soluble gliadin monomers by N-terminal amino acid sequencing and analytical ultracentrifugation. Extracted proteins were aggregated by the addition of NaCl at concentrations of >10 mM. A decrease in beta-turn structures, which expose tryptophan residues to an aqueous environment in the presence of NaCl, was revealed by Fourier transform infrared analysis and scanning of fluorescence spectra. In addition, cross-linking experiments with disuccinimidyl tartrate showed that a large amount of protein was cross-linked in the dough only in the presence of NaCl. These results suggest that both interactions and distances between proteins were altered by the addition of NaCl.
authors.affiliation: Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Gokasho, Uji, Kyoto 611-0011, Japan.
authors.forename: Tomoyo
authors.initials: T
authors.lastname: Ukai
authors.forename: Yasuki
authors.initials: Y
authors.lastname: Matsumura
authors.forename: Reiko
authors.initials: R
authors.lastname: Urade
mesh_terms: D000595:Amino Acid Sequence; D001939:Bread / Q000032:analysis; D005903:Gliadin / Q000032:analysis / Q000737:chemistry; D005983:Glutens / Q000737:chemistry* / Q000187:drug effects*; D012965:Sodium Chloride / Q000494:pharmacology*; D014461:Ultracentrifugation
chemical_list: D012965:Sodium Chloride; D005983:Glutens; D005903:Gliadin