Papaya latex enzymes capable of detoxification of gliadin

Cornell, H, Doherty, W and Stelmasiak, T 2010, 'Papaya latex enzymes capable of detoxification of gliadin', Amino Acids, vol. 38, no. 1, pp. 155-165.

Document type: Journal Article
Collection: Journal Articles

Title Papaya latex enzymes capable of detoxification of gliadin
Author(s) Cornell, H
Doherty, W
Stelmasiak, T
Year 2010
Journal name Amino Acids
Volume number 38
Issue number 1
Start page 155
End page 165
Total pages 10
Publisher Springer Wien
Abstract Assay of fractions obtained from ion exchange chromatography of papaya latex on CM Sephadex-C50, size exclusion chromatography on Sephacryl S-300 and size exclusion HPLC have provided an insight into the relative contributions of the gluten-detoxifying enzymes present. This outcome has been achieved by the use of the above chromatographic techniques, coupled with assays of lysosomal activity, protease activity using benzylarginine ethyl ester (BAEE) as substrate, prolyl endopeptidase (PEP) using glycylprolylnitroanilide and a prolidase assay using acetylprolylglycine. These procedures have shown that the activity in papaya latex is due largely to caricain and to a lesser extent, chymopapain and glutamine cyclotransferase. The presence of caricain and these other enzymes was confirmed by mass spectrometry of trypsin digests of the most active fraction obtained by CM Sephadex-C50 chromatography and size exclusion HPLC. Fractions rich in caricain would be suitable for enzyme therapy in gluten intolerance and appear to have synergistic action with porcine intestinal extracts.
DOI - identifier 10.1007/s00726-008-0223-6
Copyright notice © 2009 Springer-Verlag
ISSN 0939-4451
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Citation counts: TR Web of Science Citation Count  Cited 8 times in Thomson Reuters Web of Science Article | Citations
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