Jefferson Adams is a freelance writer living in San Francisco. His poems, essays and photographs have appeared in Antioch Review, Blue Mesa Review, CALIBAN, Hayden's Ferry Review, Huffington Post, the Mississippi Review, and Slate among others.
He is a member of both the National Writers Union, the International Federation of Journalists, and covers San Francisco Health News for Examiner.com.
Celiac.com 02/07/2008 - Are we close to finding a way for people with gluten intolerance and celiac disease to safely break down and properly digest wheat gluten and protein? An article recently published in the medical journal Gut describes the results of laboratory experiments in which doctors duplicated a human digestive tract and isolated an enzyme that degrades wheat gluten and protein. Moreover, the results show that the enzyme also eliminated the toxic response to the wheat gluten and protein common in folks with gluten intolerance and celiac disease.
According to the researchers, if a full-scale trial confirms the results, people with gluten intolerance and celiac disease might be able to safely stray from their strict gluten-free diets on occasion.
The enzyme is prolyl endoprotease isolated from Aspergillus niger and shows the power to quickly and effectively break down gluten peptides and proteins in a simulated human digestive tract. The enzyme has a similar pH level to that of the stomach, and remains intact in the stomach’s strongly acidic conditions.
The research team, led by Dr. C. Mitea from Leiden University Medical Center in the Netherlands tested the enzyme in a controlled system built to function in way that is nearly identical with the human gastrointestinal tract.
According to the report, the enzyme increased the digestion speed of the glutenins and gliadins that are found in white bread, and which people with gluten intolerance and celiac disease cannot properly break down. After 90 minutes, the gluten proteins treated with the enzyme were undetectable, whereas those glutens not treated with the enzyme, remained in the stomach for at least two hours.
The research team obtained similar results when they repeated the test on a fast food meal rather than just white bread alone, and showed that the enzyme treated food samples also eliminated adverse T-cell stimulatory activity that occurred in untreated samples. The tests showed that, in the same amount of time that food normally remains in the stomach, the enzyme brought about the total elimination of T-cell stimulatory peptides of gliadins and glutenins.
From the test results, the research team concluded that the enzyme is a solid choice for clinical trials to determine if it can eliminate 100% of gluten toxicity. They also noted that the enzyme is readily available in industrial quantities, and thus easy to tailor into a suitable treatment should trials prove fruitful.
Gut, Jan 2008; 57: 25 - 32.
Editor's Note: This is not a therapy that is designed to allow celiacs to eat gluten on a daily basis. At best it will allow them to not worry about cross-contamination when eating out.