ABSTRACT Coeliac disease is an immune‐mediated enteropathy triggered by dietary gluten in genetically predisposed individuals. Intestinal tissue transglutaminase (tTG) deamidates gluten peptides, enhancing their presentation by HLA‐DQ2/DQ8 heterodimers and promoting a T‐cell‐mediated inflammatory response. Transamidation of wheat flour by microbial transglutaminase could neutralize this inflammatory pathway. This study aimed to evaluate the effectiveness of pilot‐scale flour transamidation on the chemical, immunological, technological, and sensory properties of a first‐time‐manufactured gluten‐free wheat bread. Thirty mTG treatments showed reproducible recovery of transamidated gluten in the soluble protein fraction (spf) ( p = 0.25). LC‐MS/MS analysis confirmed the absence of the native α2‐gliadin (33mer), the most coeliacogenic peptide, in all spf preparations. Analysis of the immune response in sensitized HLA‐DQ8 transgenic mice indicated that spf did not stimulate the secretion of either adaptive (IFN‐γ, IL‐17, and IL‐10) or innate (TNF‐α) immunity markers. Assessment of technological parameters showed that a mixture of spf (10% w:w) with deglutinated wheat starch raised similarly to conventional wheat dough with main baking parameters preserved and a native gluten content <20 ppm. Texture profiling indicated that the hardness, cohesiveness, and springiness of the gluten‐free product were similar to those of conventional wheat bread. By contrast, differences in chemical composition and in the in vitro starch digestion were reported. Sensory analysis found variations among bread formulations. Importantly, wheat aroma and flavor were mainly preserved in the spf bread. In conclusion, our results highlight wheat flour transamidation as an affordable methodology both in preventing immune activity to gluten and for industrial applications.
Treppiccione et al. (Thu,) studied this question.