dc.identifier.uri |
http://dx.doi.org/10.15488/13343 |
|
dc.identifier.uri |
https://www.repo.uni-hannover.de/handle/123456789/13452 |
|
dc.contributor.author |
Ersoy, Franziska
|
|
dc.contributor.author |
Beinhorn, Philine
|
|
dc.contributor.author |
Schalk, Kathrin
|
|
dc.contributor.author |
Scherf, Katharina A.
|
|
dc.contributor.author |
Berger, Ralf G.
|
|
dc.contributor.author |
Krings, Ulrich
|
|
dc.date.accessioned |
2023-03-21T06:08:04Z |
|
dc.date.available |
2023-03-21T06:08:04Z |
|
dc.date.issued |
2023 |
|
dc.identifier.citation |
Ersoy, F.; Beinhorn, P.; Schalk, K.; Scherf, K.A.; Berger, R.G.et al.: A Prolyl Endopeptidase from Flammulina velutipes Degrades Celiac Disease-Inducing Peptides in Grain Flour Samples. In: Catalysts : open access journal 13 (2023), Nr. 1, 158. DOI: https://doi.org/10.3390/catal13010158 |
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dc.description.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. |
eng |
dc.language.iso |
eng |
|
dc.publisher |
Basel : MDPI |
|
dc.relation.ispartofseries |
Catalysts : open access journal 13 (2023), Nr. 1 |
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dc.rights |
CC BY 4.0 Unported |
|
dc.rights.uri |
https://creativecommons.org/licenses/by/4.0/ |
|
dc.subject |
Basidiomycete |
eng |
dc.subject |
Flammulina velutipes |
eng |
dc.subject |
prolyl endopeptidase |
eng |
dc.subject |
celiac disease |
eng |
dc.subject |
gliadin |
eng |
dc.subject |
hordein |
eng |
dc.subject |
secalin |
eng |
dc.subject |
33-mer |
eng |
dc.subject.ddc |
540 | Chemie
|
ger |
dc.title |
A Prolyl Endopeptidase from Flammulina velutipes Degrades Celiac Disease-Inducing Peptides in Grain Flour Samples |
|
dc.type |
Article |
|
dc.type |
Text |
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dc.relation.essn |
2073-4344 |
|
dc.relation.doi |
https://doi.org/10.3390/catal13010158 |
|
dc.bibliographicCitation.issue |
1 |
|
dc.bibliographicCitation.volume |
13 |
|
dc.bibliographicCitation.firstPage |
158 |
|
dc.description.version |
publishedVersion |
|
tib.accessRights |
frei zug�nglich |
|