Determination of celiac disease-specific peptidase activity of germinated cereals |
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Authors: | Benedict?Ge?endorfer Georg?Hartmann Herbert?Wieser Email author" target="_blank">Peter?KoehlerEmail author |
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Affiliation: | 1.Deutsche Forschungsanstalt für Lebensmittelchemie,Freising,Germany;2.aromaLAB AG,Freising,Germany;3.HiPP GmbH & Co. KG,Pfaffenhofen,Germany |
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Abstract: | A method to determine the celiac disease-specific peptidase activity of different germinated cereals was developed. Kernels
of common wheat, spelt, emmer, einkorn, rye, and barley were germinated, lyophilized, and milled into flour and bran. The
latter was extracted at pH 4.0 to obtain a solution enriched with peptidases. The synthetic α-gliadin peptide with the amino
acid sequence PQPQLPYPQPQLPY (peptide IV), which has been shown to be toxic for celiac disease patients, was selected as substrate
for bran peptidases. It was quantified by reversed-phase high-performance liquid chromatography on C18 silica gel. For kinetic studies, rye bran extract was incubated with peptide IV at 50 °C and pH 6.5. The peptide was degraded
continuously, and only 30.2% of the original peptide was detected after 90 min. Accordingly, the bran extracts of all cereals
were investigated. The incubation time was set to 60 min at 50 °C, and the degradation of peptide IV was performed at pH 4.0
and 6.5, respectively. Except for rye, peptide degradation was faster at pH 4.0 than at pH 6.5. At pH 4.0, emmer extract was
most active, followed by spelt, common wheat, and einkorn extracts. The activity of rye and barley extracts was significantly
lower. In conclusion, the method is easy to perform, quick, and provides reproducible results. It can be applied to other
peptidase sources such as bacterial or fungal cultures to optimize peptidase preparations suitable for detoxifying gluten-containing
food or for drugs to treat celiac disease. |
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