(P06-008-23) A Supplemental Mixture of Microbial and Plant Proteases Promotes Protein Digestion From Gluten-Rich Foods Under Simulated Gastrointestinal Conditions

Objectives: Consumption of foods containing gluten proteins is associated with gastrointestinal (GI) symptoms in individuals with non-celiac gluten sensitivity (NCGS). Individuals with NCGS typically benefit from a gluten-free diet, however, this dietary change is difficult to implement. An additional approach is enzyme supplementation targeting gluten hydrolysis. The objective of this study was to test the effects of OPTIZIOME® GluteAX®, a mixture of three microbial proteases and papain (a plant protease), on the digestion of gluten-rich foods in the INFOGEST in vitro static simulation of GI digestion.

Methods: Substrates included whole wheat cereal (Weetabix®) and whole wheat couscous (Bob’s Red Mill®). The predominant wheat gluten protein called alpha-gliadin is comprised of 40% glutamine and 12% leucine. The concentration of these unbound, free amino acids, as well as the total of all 20 amino acids (TAA), were measured in gastric and intestinal digestas by HPLC to determine GluteAX®’s efficacy. The free amino nitrogen (FAN) concentration of gastric digestas was also measured by spectrophotometry.

Results: Following simulated salivary-gastric digestion of whole wheat cereal, the TAA and FAN concentrations of gastric digestas were 50% and > 10-fold higher, respectively, with GluteAX® treatment compared to pepsin-only controls (TAA, P = 0.0032; FAN, P = 0.0044). With couscous, the TAA and FAN concentrations of gastric digestas were 4- and 6-fold higher with GluteAX® treatment compared to controls (TAA, P = 0.0260; FAN, P < 0.0001). Compared to controls, GluteAX® treatment also yielded increased gastric digesta concentrations of free glutamine (wheat, P = 0.0276; couscous, P = 0.0072) and free leucine (wheat, P = 0.0002; couscous, P = 0.0102). Following the salivary-gastric-intestinal simulation, neither TAA nor FAN concentrations of intestinal digestas treated with GluteAX® showed any differences from controls, suggesting that endogenous pancreatin masked any further effects of GluteAX® on gluten digestion in the intestinal phase.

Conclusions: These in vitro data support use of supplemental microbial and plant enzymes to promote gluten digestion in the stomach before transit to the intestine. Future experimentation by LC-MS will test GluteAX® efficacy on hydrolysis of digestion-resistant alpha-gliadin peptides.

Funding Sources: BIO-CAT, Inc.