Reduction of toxic gliadin content of wholegrain bread by the enzyme caricain

Buddrick, O, Cornell, H and Small, D 2014, 'Reduction of toxic gliadin content of wholegrain bread by the enzyme caricain', Food Chemistry, vol. 170, pp. 343-347.

Document type: Journal Article
Collection: Journal Articles

Title Reduction of toxic gliadin content of wholegrain bread by the enzyme caricain
Author(s) Buddrick, O
Cornell, H
Small, D
Year 2014
Journal name Food Chemistry
Volume number 170
Start page 343
End page 347
Total pages 5
Publisher Elsevier
Abstract Increasingly the number of individuals being diagnosed with some form of sensitivity to the proteins in wheat grains represents a cause for concern. Currently, the treatment is dietary withdrawal of gluten, but commercial gluten-free bread presents some undesirable properties. The objective of this study has been to assess the ability of the enzyme caricain (from papaya latex) to detoxify gliadin in whole wheat flour and develop bread suitable for coeliacs and gluten intolerant individuals. Ion exchange chromatography was used to enrich the caricain in papaya latex and an enzyme-linked immunosorbent assay test kit was used for the analysis of gliadin residues in the baked bread. The partially purified enzyme was found to be more effective in reducing gliadin content than the crude papain and the resultant loaves had acceptable crumb and crust characteristics. Caricain appears to be capable of detoxifying gliadin and has the potential to mitigate the problems confronting coeliacs.
Subject Food Sciences not elsewhere classified
Keyword(s) Caricain
Coeliac disease
Gluten intolerance
DOI - identifier 10.1016/j.foodchem.2014.08.030
Copyright notice © 2014 Elsevier Ltd. All rights reserved.
ISSN 0308-8146
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Citation counts: TR Web of Science Citation Count  Cited 11 times in Thomson Reuters Web of Science Article | Citations
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