Glutathione changes physical properties of rice batter without increasing its allergenicity

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In our previous studies, glutathione, a biologically ubiquitous tripeptide, has been shown to improve swelling of glutenfree rice bread. To further characterize the effects of glutathione, we studied structural changes in batter protein in relation to gas retention properties of the batter. Glutathione (just as dithiothreitol and cysteine) cleaved the glutelin polymers into monomers, and concurrently improved gas retention capacity of the rice batter. Moreover, glutathione apparently did not promote formation of disulfide bonds among proteins. This was in contrast to wheat dough where extensive intermolecular disulfide bonds among proteins formed during kneading. Besides, an allergenicity test involving serum samples from dogs with wheat allergy suggested that the use of glutathione did not increase allergenicity of gluten-free rice bread. Our results suggest that glutathione modestly changes the structure of food protein while improving the physical properties of food without increasing its allergenicity. Our findings show usefulness of glutathione for research into the development of new foods.

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