期刊
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
卷 65, 期 34, 页码 7542-7552出版社
AMER CHEMICAL SOC
DOI: 10.1021/acs.jafc.7b02557
关键词
acyl-acceptor molecule; gliadin; immunogenic properties; microbial transglutaminase; transamidation
资金
- International Science & Technology Cooperation Program of China [2013DFG31380]
Wheat gluten confers superior baking quality to wheat based products but elicits a pro-inflammatory immune response in patients-with celiac disease. Transamidation.of gluten by microbial transglutaminase (mTG) and tissue transglutaminase (tTG) reduces the immunogenicity of gluten; however, little information is available on the minimal modification sufficient to eliminate gliadin immunogenicity nor has the effectiveness of transamidation been studied with T-cell clones from patients. Here we demonstrate that mTG can efficiently couple three different aryl-acceptor molecules, L-lysine, glycine ethyl ester, and hydroxylamine, to gliadin peptides and protein. While all three aryl-acceptor molecules were cross-linked to the same Q-residues, not all modifications were equally effective in silencing T-cell reactivity. Finally, we observed that tTG can partially reverse the mTG-catalyzed transamidation by its isopeptidase activity. These results set the stage to determine the impact of these modifications on the baking quality of gluten proteins and in vivo immunogenicity of such food products.
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