A Prolyl Endopeptidase from Flammulina velutipes Degrades Celiac Disease-Inducing Peptides in Grain Flour Samples

Celiac disease (CD) is an inflammatory disorder of the small intestine. Gluten peptides are supposed to be responsible for reaction, best-researched which so-called ‘33-mer’. Analogous in secalins (rye) and hordeins (barley) have been described. This study presents degradation gliadins, glutenins, purified from respective flours using a prolyl endopeptidase Basidiomycete Flammulina velutipes (FvpP). The flour fractions were incubated with enzyme, cleavage sites determined high-resolution nLC-qTOF-MS/MS. For wheat samples, eight 33-mer peptide shown, all six described epitopes successfully cleaved. commercially available prolyl-specific Aspergillus niger (An-Pep), was used as control, only two that cleaved three identified. secalins, four CD-active QPFPQPQQPIPQ found FvpP but none An-Pep. QPFPQPEQPFPW C-hordein at positions by FvpP. proves usability degrade CD-inducing real-grain samples indicates its higher effectiveness compared A clinical would required assess therapeutic or preventive potential CD.