ABSTRACT Coeliac disease (CD) is caused by immunological intolerance to wheat gluten and related proteins of rye and barley. Consequently, gluten-free (GF) products have been developed but technological implementation is… Click to show full abstract
ABSTRACT Coeliac disease (CD) is caused by immunological intolerance to wheat gluten and related proteins of rye and barley. Consequently, gluten-free (GF) products have been developed but technological implementation is required to improve their intrinsic rheological properties. One alternative for increasing the functional properties of GF foodstuff is the incorporation of microbial transglutaminase (mTG), which allows for the cross-linking of proteins that can substitute for the gluten network in the bakery industry. mTG has been, however, suggested to mimic tissue transglutaminase and to be immunogenic in CD patients. Recently, both mTG and gliadin were found to be transported to the endoplasmic reticulum of enterocytes, suggesting cross-presentation and potential interaction with immune cells in CD. Although pathogenetic activity of mTG has not been found to date, these data naturally raise concerns among clinicians and patients about the use of mTG as a food additive. On the contrary, different studies have shown that treatment with mTG was effective in reducing the inflammatory immune response of gluten in CD. In this article, we take advantage of recent advances in gut physiology and CD pathogenesis to revise the literature data on mTG. An updated and unbiased overview of the role of mTG in this pathology allowed us to definitively highlight the beneficial use of this food additive by CD patients.
               
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