An enzyme that degrades gluten might offer possible benefits to people who need to follow a gluten-free diet. But is it really effective?
For people who can’t eat gluten, dining out or attending a party can be a nerve-racking experience.
They can avoid foods containing gluten, but there is always a risk that trace amounts may exist in what they consume.
“They can’t be 100 percent sure that the meals they are served are free of gluten,” Julia König, PhD, a post-doctoral research fellow at the School of Medical Sciences at University of Örebro, Sweden, said in a conference call.
König is the lead author of a new study on a gluten-destroying enzyme that could potentially make a difference in the lives of cautious diners.
Among people who follow a gluten-free diet, some are more sensitive to cross-contamination than others.
People with celiac disease, an autoimmune condition, generally can’t tolerate even tiny amounts of gluten.
Those who don’t have celiac disease may still be considered “gluten sensitive” if eating gluten causes negative symptoms, such as bloating, diarrhea, and abdominal pain.
Even if a gluten-sensitive person chooses gluten-free foods, the food may be contaminated by other foods containing gluten, resulting in a bad reaction.
But the enzyme König studied might provide a protective benefit because it prevents a significant amount of gluten from going into the small intestine and causing discomfort.
“Since even small amounts of gluten can affect gluten-sensitive patients, this supplement can play an important role in addressing the residual gluten that is often the cause of uncomfortable symptoms,” she stated in a press release.
König’s results were presented at Digestive Disease Week (DDW) 2017.
The enzyme — known as AN-PEP, a prolyl endoprotease — was found in previous research to be able to break down gluten when it was tested in a feeding tube.
König’s latest study involved 18 people with gluten sensitivities who ate a meal of porridge and other foods including gluten-containing wheat cookies.
The study participants also took either a high-dose or a low-dose of AN-PEP, or a placebo.
The researchers then examined the gluten levels in the participants’ bodies over a three-hour span.
They found that the enzyme broke down gluten in the stomach and the first section of the small intestine, known as the duodenum.
In patients who took AN-PEP, gluten levels in their stomachs were 85 percent lower than in those who took a placebo.
By the time the food reached the duodenum, gluten levels declined by 81 percent in the high-dose group and 87 percent in the low-dose group compared to those who took the placebo.
“While the researchers did note an 81 to 87 percent reduction in gluten levels, this still leaves a residual amount of 13 to 19 percent of gluten in the system,” Dr. Amy Burkhart, a doctor and dietitian from California, who also has celiac disease, told Healthline. “Depending on the initial dose of gluten, this amount of residual could be harmful to a patient with celiac disease.”
AN-PEP was not tested in people with celiac disease because even small amounts of gluten can cause long-term harm.
König pointed out that the enzyme isn’t designed to treat or prevent gluten sensitivity, or celiac disease, but it may be a good option for people who are gluten sensitive to have on hand if they unintentionally interact with gluten.
Those people should still remain on a gluten-free diet, she said.
“There are many non-celiac gluten-sensitive patients who are not concerned or symptomatic with small amounts of gluten exposure,” Burkhart added. “The evidence is not clear that this population needs to adhere to a gluten-free diet as strictly as someone with celiac disease.”
This isn’t the first time an enzyme has been tested to break down gluten, but König noted that others have not been tested in humans as her study did with AN-PEP.
AN-PEP is currently available in the United States. It’s produced by the Dutch firm DSM and sold under the name Tolerase.
Dr. Alessio Fasano, director of the Center for Celiac Research and Treatment at Massachusetts General Hospital, said the findings were not significant.
He said the way they were presented in the study’s press release could be dangerous, giving “false hope and confidence” to people with celiac disease that using the enzyme is a safety net.
“I think that defining these findings as possible ‘game-changers’ is a bold statement based on what we have learned over the years on the efficacy of prolyl endopeptidases to detoxify gluten,” Fasano told Healthline.
Further studies and clinical trials did not show data differences between people who took AN-PEP compared to those who took a placebo.
Fasano explained that there are other technologies in the research pipeline that are in “a much more advanced phase.”
For example, a vaccine currently being tested is one of the “most promising” therapies on the horizon, Burkhart added.
It works in a similar way to allergy injections, as it is aimed at helping people with celiac disease develop a tolerance to gluten.
But until such therapies are available, gluten-free diners may have to make do with cautious meal planning.