Release and conformational changes in allergenic proteins from wheat gluten induced by high hydrostatic pressure

Abstract

The gluten proteins of wheat are major causative agents of harmful immune responses. This study investigated the effects of high hydrostatic pressure (200, 300, 400, and 500 MPa), treatment time (5–25 min) and protein concentration (1%-5% protein weight/volume) on the structures underlying the allergenicity wheat gluten. The results showed that a combination of 400 MPa, 20 min treatment time and 3% protein reduced the wheat gluten allergenicity by 72.2%. Moreover, a Western blotting showed that the allergenicity of 26, 28, 48, 68 kDa and high molecular weight glutenin was sharply reduced. Fourier infrared spectroscopy and surface hydrophobicity indicated that gluten molecules aggregated after HHP treatment. Intermolecular forces indicated that gluten aggregated mainly through hydrophobic interactions and disulfide bonds but not by hydrogen bonds after HHP treatment. These results suggest that structural changes contributed to the reduction of wheat gluten allergenicity and that HHP may enhance safety for susceptible individuals.