Celiac.com 10/23/2015 - Just as I finished writing about the failure of current commercial enzymes to effectively degrade gluten, an interesting study on another enzyme suggests that there may be help on the horizon, at least for people without celiac disease.
According to the latest press release, in lab conditions, aspergillus niger prolyl endoprotease (AN-PEP) efficiently degrades gluten molecules into non-immunogenic peptides. But so what?
If AN-PEP is to be effective in people with celiac disease or gluten-sensitivity, which would seem to be the whole point of an anti-gluten enzyme, it must effectively digest gluten in "non-healthy" subjects.
A team of researchers recently set out to assess AN-PEP on gluten degradation in a low and high calorie meal in healthy...

Celiac.com 10/21/2016 - Researchers at Boston University's Henry M. Golden School of Dental Medicine have identified a metabolic enzyme that alerts the body to invading bacteria, which may lead to new treatments for celiac disease.
A research team that set out to isolate and identify the enzymes and evaluate their potential as novel enzyme therapeutics for celiac disease, reports that the enzymes exhibit exceptionally high gluten-degrading enzyme activities, and are "naturally associated with bacteria that colonize the oral cavity."
Rothia bacteria, found in human saliva, can break down gluten compounds that cause an exaggerated immune response and that are typically resistant to the digestive enzymes that mammals produce. The team was able to isolate a new class of gluten-degrading...

Celiac.com 12/26/2016 - Could gluten-degrading enzymes offer a better future for celiac patients? Rothia mucilaginosa is an oral microbial colonizer that can break down proline- and glutamine-rich proteins present in wheat, barley, and rye that contain the immunogenic sequences that drive celiac disease. A team of researchers recently set out to isolate and identify the enzymes and evaluate their potential as novel enzyme therapeutics for celiac disease.
The research team included G Wei, N Tian, R Siezen, D Schuppan, and EJ Helmerhorst. They are variously affiliated with the Department of Molecular and Cell Biology at the Henry M. Goldman School of Dental Medicine in Boston, Massachusetts; the Bacterial Genomics Group, Center for Molecular and Biomolecular Informatics at Radboud University...

Celiac.com 04/29/2020 - People with celiac disease cannot eat gluten from products made with wheat, barley or rye.  The two main culprits proteins in gluten are glutenin and gliadin, with the latter thought to cause most of the inflammation and adverse health health effects in people with celiac disease. Glutenases are enzymes needed to break down glutens in foods to make these foods easier for people to digest.
Imagine an enzyme that could be added to traditional wheat or gluten-containing products to make them gluten-free. The technology would work very much the way adding lactase to regular milk breaks down the lactose proteins and makes the milk safe for people with milk intolerance.
It's a very cool idea. One major hurdle involves the fact that glutenase enzymes that ...