Reduction of toxic gliadin content of wholegrain bread by the enzyme caricain.
Food Chem
; 170: 343-7, 2015 Mar 01.
Article
en En
| MEDLINE
| ID: mdl-25306355
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.
Palabras clave
Texto completo:
1
Bases de datos:
MEDLINE
Asunto principal:
Proteínas de Plantas
/
Pan
/
Ensayo de Inmunoadsorción Enzimática
/
Cisteína Endopeptidasas
/
Harina
/
Gliadina
/
Glútenes
Límite:
Humans
Idioma:
En
Revista:
Food Chem
Año:
2015
Tipo del documento:
Article
País de afiliación:
Australia