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

• Crude papain was able to detoxify wheat dough.
• Caricain partially purified from papain by ion exchange showed enhanced detoxification.
• Effective detoxification was achieved with 5 h fermentation.

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.