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- Title
A Prolyl Endopeptidase from Flammulina velutipes Degrades Celiac Disease-Inducing Peptides in Grain Flour Samples.
- Authors
Ersoy, Franziska; Beinhorn, Philine; Schalk, Kathrin; Scherf, Katharina A.; Berger, Ralf G.; Krings, Ulrich
- Abstract
Celiac disease (CD) is an inflammatory disorder of the small intestine. Gluten peptides are supposed to be responsible for the reaction, the best-researched of which is the so-called '33-mer'. Analogous peptides in secalins (rye) and hordeins (barley) have been described. This study presents the degradation of gliadins, glutenins, hordeins and secalins purified from the respective flours using a prolyl endopeptidase from the Basidiomycete Flammulina velutipes (FvpP). The flour fractions were incubated with the enzyme, and the cleavage sites were determined using high-resolution nLC-qTOF-MS/MS. For the wheat samples, eight cleavage sites in the 33-mer peptide were shown, and all of the six described epitopes were successfully cleaved. For the commercially available prolyl-specific endopeptidase from Aspergillus niger (An-Pep), which was used as a control, only two cleavage sites that cleaved three of the six epitopes were identified. For the secalins, four prolyl-specific cleavage sites in the CD-active peptide QPFPQPQQPIPQ were found for the FvpP but none for the An-Pep. The CD-active peptide QPFPQPEQPFPW in C-hordein was cleaved at three prolyl-specific positions by the FvpP. The study proves the usability of FvpP to degrade CD-inducing peptides in real-grain flour samples and indicates its higher effectiveness compared with An-Pep. A clinical study would be required to assess the therapeutic or preventive potential of FvpP for CD.
- Subjects
FLAMMULINA velutipes; PEPTIDES; GLUTELINS; GLIADINS; CELIAC disease; GRAIN; FLOUR
- Publication
Catalysts (2073-4344), 2023, Vol 13, Issue 1, p158
- ISSN
2073-4344
- Publication type
Article
- DOI
10.3390/catal13010158