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Sourdough fermentation of wheat flour does not prevent the interaction of transglutaminase 2 with α2-gliadin or gluten.
Nutrients. 2015 Mar 25; 7(4):2134-44.N

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.

Authors+Show Affiliations

Division of Food and Nutrition Science, Department of Biology and Biological Engineering, Chalmers University of Technology, S-412 96 Gothenburg, Sweden. niklas.engstrom@chalmers.se.Division of Food and Nutrition Science, Department of Biology and Biological Engineering, Chalmers University of Technology, S-412 96 Gothenburg, Sweden. ann-sofie.sandberg@chalmers.se.Division of Food and Nutrition Science, Department of Biology and Biological Engineering, Chalmers University of Technology, S-412 96 Gothenburg, Sweden. nathalie.scheers@chalmers.se.

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

25816160

Citation

Engström, Niklas, et al. "Sourdough Fermentation of Wheat Flour Does Not Prevent the Interaction of Transglutaminase 2 With Α2-gliadin or Gluten." Nutrients, vol. 7, no. 4, 2015, pp. 2134-44.
Engström N, Sandberg AS, Scheers N. Sourdough fermentation of wheat flour does not prevent the interaction of transglutaminase 2 with α2-gliadin or gluten. Nutrients. 2015;7(4):2134-44.
Engström, N., Sandberg, A. S., & Scheers, N. (2015). Sourdough fermentation of wheat flour does not prevent the interaction of transglutaminase 2 with α2-gliadin or gluten. Nutrients, 7(4), 2134-44. https://doi.org/10.3390/nu7042134
Engström N, Sandberg AS, Scheers N. Sourdough Fermentation of Wheat Flour Does Not Prevent the Interaction of Transglutaminase 2 With Α2-gliadin or Gluten. Nutrients. 2015 Mar 25;7(4):2134-44. PubMed PMID: 25816160.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Sourdough fermentation of wheat flour does not prevent the interaction of transglutaminase 2 with α2-gliadin or gluten. AU - Engström,Niklas, AU - Sandberg,Ann-Sofie, AU - Scheers,Nathalie, Y1 - 2015/03/25/ PY - 2014/10/15/received PY - 2015/03/19/accepted PY - 2015/3/28/entrez PY - 2015/3/31/pubmed PY - 2016/1/28/medline SP - 2134 EP - 44 JF - Nutrients JO - Nutrients VL - 7 IS - 4 N2 - 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. SN - 2072-6643 UR - https://www.unboundmedicine.com/medline/citation/25816160/Sourdough_fermentation_of_wheat_flour_does_not_prevent_the_interaction_of_transglutaminase_2_with_α2_gliadin_or_gluten_ L2 - https://www.mdpi.com/resolver?pii=nu7042134 DB - PRIME DP - Unbound Medicine ER -