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Improvement of Digestibility, Reduction in Allergenicity, and Induction of Oral Tolerance of Wheat Gliadin by Deamidation
Author(s) -
Hitomi Kumagaı,
Akihiro Suda,
Hidetoshi Sakurai,
Hitoshi Kumagai,
Soichi Arai,
Naoko Inomata,
Zenrō Ikezawa
Publication year - 2007
Publication title -
bioscience biotechnology and biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.509
H-Index - 116
eISSN - 1347-6947
pISSN - 0916-8451
DOI - 10.1271/bbb.60645
Subject(s) - gliadin , deamidation , chemistry , food science , biochemistry , gluten , enzyme
Wheat gliadin was deamidated by using a cation-exchange resin in the presence or absence of added cysteine, with the change in digestibility being measured. The allergenicity of the gliadin was evaluated by using sera from patients RAST-positive to wheat. Gliadin-specific IgE was measured after the gliadin had been orally administered to rats. The addition of cysteine before the treatment with a cation exchanger effectively increased the deamidation level of gliadin. Deamidated gliadin showed higher solubility than the undeamidated form. There was no difference in the peptic digestibility of the gliadin, whereas deamidation enhanced the pancreatic digestibility in vitro and the digestibility in the mouse stomach in vivo. Deamidation of gliadin reduced its reactivity toward the sera of patients with wheat allergy. Rats administered with deamidated gliadin showed suppressed elevation of the gliadin-specific IgE level.

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