Disaggregation and reaggregation of gluten proteins by sodium chloride

Journal of Agricultural and Food Chemistry
Tomoyo UkaiReiko Urade

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.

Citations

Jun 27, 2013·Journal of Agricultural and Food Chemistry·Tabea PflaumPeter Koehler
Dec 10, 2015·Bioscience, Biotechnology, and Biochemistry·Takenobu Ogawa, Shuji Adachi
Jun 28, 2012·Biotechnology Progress·Hiroyuki NagaokaKohtaro Kirimura
Mar 19, 2013·Food Chemistry·J Miedzianka, A Pęksa
Dec 4, 2020·Food Chemistry·E Abedi, K Pourmohammadi
Jan 9, 2021·Journal of the Science of Food and Agriculture·Kexin MengTongchao Su
Nov 20, 2010·Journal of Agricultural and Food Chemistry·Akie KohReiko Urade
Sep 24, 2014·Journal of Agricultural and Food Chemistry·Xiaoming WangZhaoxin Lu

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