Improvement of Digestibility, Reduction in Allergenicity, and Induction of Oral Tolerance of Wheat Gliadin by Deamidation

Impact of urban air pollution on the allergenicity of Aspergillus fumigatus conidia: Outdoor exposure study supported by laboratory experiments

“…Deamidation was previously shown to reduce allergenicity of the wheat allergen gliadin (Kumagai et al, 2007), indicative of the cause leading to the reduction in their activity with exposure time. Deamidation leads to an alteration of asparagine and glutamate residue to a mixture of isoaspartate and aspartate or isoglutamate and glutamate, respectively (Robinson and Rudd, 1974).…”

Evaluation of Reduced Allergenicity of Deamidated Gliadin in a Mouse Model of Wheat-Gliadin Allergy Using an Antibody Prepared by a Peptide Containing Three Epitopes

“…29 Thus, a further reduction in its allergenicity may occur during digestion. This study was therefore conducted to examine the in vivo allergenicity of DG by using wheat-allergy model mice.…”

“…25−30 Since cation-exchange resins are resistant to ethanol, this method is applicable to the deamidation of ethanol-soluble proteins such as gliadins. 25,29 The deamidated gliadin obtained by this technique showed higher foaming property than egg-white albumin and globulin; this property may improve the texture of bakery products such as bread and cakes. Deamidation increased the solubility of gliadin in water and salt solutions, which led to improved digestibility.…”

Chemical and Enzymatic Protein Modifications and Functionality Enhancement

“…The amino acid cysteine can also be used for de-cross-linking by forming disulfide bonds between the cysteine residue of a protein and the amino acid, cysteine. Protein unfolding often occurs by this de-crosslinking, and becomes more susceptible to the reaction (Kumagai et al 2007). …”

“…As cereal, pulse, and seed proteins are abundant in acid amides, wheat protein (Matsudomi, Kato, and Kobayashi 1982;Matsudomi et al 1986;Bollecker et al 1990;Hamada 1991b;Izzo, Lincoln, and Ho 1993;Zhang, Lee, and Ho 1993;Yong, Yamaguchi, and Matsumura 2006;Kumagai et al 2007), soybean protein (Shih 1987(Shih , 1990(Shih , 1991Kato et al 1987aKato et al , 1987bMarshall 1988, 1989;Hamada 1991aHamada , 1991bZhang, Lee, and Ho 1993;Guéguen 1995, 1999;Kumagai et al , 2004, corn protein (Hamada 1991b;Yong et al 2004), egg protein (Kato et al 1987a(Kato et al , 1987bHamada 1991b), milk protein (Motoki et al 1986;Hamada 1991b;Gu et al 2001), oilseed protein (Shih and Kalmar 1987), canola protein (Igor, Diosady, and Rubin 1993), and oat protein (Ma and Khanzada 1987) are mainly deamidated to improve their functionality.…”