Scott Adams

In 1994 I was diagnosed with celiac disease, which led me to create Celiac.com in 1995. I created this site for a single purpose: To help as many people as possible with celiac disease get diagnosed so they can begin to live happy, healthy gluten-free lives. Celiac.com was the first site on the Internet dedicated solely to celiac disease, and since then it has become an invaluable resource to people worldwide who seek information about celiac disease and the gluten-free diet.

In 1998 I created The Gluten-Free Mall, Your Special Diet Superstore! which was also another Internet first—it was the first gluten-free food site to offer a shopping cart-style interface, and the ability for people to order gluten-free products manufactured by many different companies at a single Web site.

I am also co-author of the book Cereal Killers, and founder and publisher of Journal of Gluten Sensitivity.

Published on 09/12/2006

Celiac.com 09/12/2006 – A recent study by researchers at Stanford University has found that

Barley Enzymes Effectively Digest Gluten in Rats

Celiac.com 09/12/2006 – A recent study by researchers at Stanford University has found that barley endoprotease EP-B2 is effective at digesting gluten in rats, and should be studied further as an “adjunct to diet control” in human celiac disease patients. This new finding adds to Stanford’s growing body of work on enzyme therapy as a possible treatment for those with celiac disease, and may one day lead to a effective treatment.

Effect of barley endoprotease EP-B2 on gluten digestion in the intact rat.
J Pharmacol Exp Ther. 2006 Sep;318(3):1178-86.
Gass J, Vora H, Bethune MT, Gray GM, Khosla C.
Stanford University.

Abstract:
"Celiac Sprue is a multi-factorial disease characterized by an intestinal inflammatory response to ingested gluten. Proteolytically resistant gluten peptides from wheat, rye and barley persist in the intestinal lumen, and elicit an immune response in genetically susceptible individuals. Here we demonstrate the in vivo ability of a gluten-digesting protease ("glutenase") to accelerate the breakdown of a gluten-rich solid meal. The proenzyme form of endoprotease B, isoform 2 from Hordeum vulgare (EP-B2) was orally administered to adult rats with a solid meal containing 1 g gluten. Gluten digestion in the stomach and small intestine was monitored as a function of enzyme dose and time by HPLC and mass spectrometry. In the absence of supplementary EP-B2, gluten was solubilized and proteolyzed to a limited extent in the stomach, and was hydrolyzed and assimilated mostly in the small intestine. In contrast, EP-B2 was remarkably effective at digesting gluten in the rat stomach in a dose and time dependent fashion. At a 1:25 EP-B2:gluten dose, the gastric concentration of the highly immunogenic 33-mer gliadin peptide reduced by more than 50-fold within 90 min, with no overt signs of toxicity. Evaluation of EP-B2 as an adjunct to diet control is therefore warranted in celiac patients."