NEW YORK (Reuters Health) - An enzyme has been recently identified that is able to degrade gluten in a laboratory simulation of the gastrointestinal tract.
If clinical trials bear out the findings, adding the enzyme to gluten-containing meals “might eliminate gluten toxicity, thus offering patients the possibility of abandoning (occasionally) their strict gluten-free diet,” write the authors.
The enzyme, a prolyl endoprotease from Aspergillus niger, was recently shown to efficiently degrade gluten peptides and proteins in laboratory experiments, the authors explain. The enyzme’s pH is compatible with that found in the stomach, and it is not broken down by gastric acid in the stomach.
Dr. C. Mitea from Leiden University Medical Center, the Netherlands and associates tested the enzyme in a system designed to closely mimic the human gastrointestinal tract, according to their report, published in the medical journal Gut.
The enzyme accelerated the digestion of glutenins and gliadins that are found in white bread, the authors report. After 90 minutes, the gluten proteins could no longer be detected. Without the enzyme, glutens persisted in the stomach for at least 120 minutes.
Similar results were obtained when a fast food meal was tested instead of white bread alone, the investigators say.
This enzyme treatment also completely abolished T-cell stimulatory activity found in untreated samples, the report indicates.
The results demonstrate that in the time that food is normally in the stomach, the enyzme led to “a complete disappearance of T-cell stimulatory peptides of gliadins and glutenins,” the authors conclude.
They believe that this enzyme is a good candidate for clinical trials to see if it can remove all gluten toxicity, the researchers conclude. They add that the enzyme is available on an industrial scale.
SOURCE: Gut, January 2008.