Abstract
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.
Highlights
Celiac DiseaseCeliac disease (CD) is a disease with an autoimmune component in tissue transglutaminase, which is initiated by the ingestion of gluten proteins in wheat and related proteins in barley (hordeins) and rye (secalins) in genetically predisposed individuals
4 × 107–9 × 108 cells/mL dough was added to each sourdough as estimated by the Colony forming units (CFU) count
L. pentosus decreased the available transglutaminase 2 (TG2) binding sites on α2-gliadin, the extent (27% ± 21%) is not sufficient to be of any importance in the aim to use lactic fermentation as a means to detoxify gluten in wheat flour
Summary
Celiac disease (CD) is a disease with an autoimmune component in tissue transglutaminase, which is initiated by the ingestion of gluten proteins in wheat and related proteins in barley (hordeins) and rye (secalins) in genetically predisposed individuals. The majority of patients will experience an improvement in their physical and psychological condition after starting on a gluten-free diet, which to date is the only treatment available [2]. The main genetic risk factors for developing CD are the genotypes encoding for the HLA class II molecules HLA-DQ2 and HLA-DQ8, where the majority of patients carry the DQ2 heterodimer [3,4]. Other factors thought to increase the risk for developing CD are various types of infections and the age of gluten introduction [6,7,8,9]. CD can be diagnosed at any age but it is most commonly discovered at early childhood, following the introduction of gluten in the diet, and at around the age of 40 and 50 for women and men, respectively [10,11]
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