Sourdough Fermentation of Wheat Flour does not Prevent the Interaction of Transglutaminase 2 with α2-Gliadin or Gluten

Nutrients

Niklas Engström¹  Ann-Sofie Sandberg² 

[1] Division of Food and Nutrition Science, Department of Biology and Biological Engineering, Chalmers University of Technology, S-412 96 Gothenburg, Sweden;

关键词: celiac disease;    gluten intolerance;    lactic fermentation;    sourdough;    G12 antibody;    tissue transglutaminase;    TG2;    QLP;    α₂-gliadin;   

DOI  :  10.3390/nu7042134

来源: mdpi

【 摘 要 】

The enzyme transglutaminase 2 (TG2) plays a crucial role in the initiation of celiac disease by catalyzing the deamidation of gluten peptides. In susceptible individuals, the deamidated peptides initiate an immune response leading to celiac disease. Several studies have addressed lactic fermentation plus addition of enzymes as a means to degrade gluten in order to prevent adverse response in celiacs. Processing for complete gluten degradation is often harsh and is not likely to yield products that are of comparable characteristics as their gluten-containing counterparts. We are concerned that incomplete degradation of gluten may have adverse effects because it leads to more available TG2-binding sites on gluten peptides. Therefore, we have investigated how lactic acid fermentation affects the potential binding of TG2 to gluten protein in wheat flour by means of estimating TG2-mediated transamidation in addition to measuring the available TG2-binding motif QLP, in α₂-gliadin. We show that lactic fermentation of wheat flour, as slurry or as part of sourdough bread, did not decrease the TG2-mediated transamidation, in the presence of a primary amine, to an efficient level (73%–102% of unfermented flour). Nor did the lactic fermentation decrease the available TG2 binding motif QLP in α₂-gliadin to a sufficient extent in sourdough bread (73%–122% of unfermented control) to be useful for celiac safe food.

【 授权许可】

CC BY   
© 2015 by the authors; licensee MDPI, Basel, Switzerland.