Screening of gluten hydrolyzing strains for food applications

Abstract

Wheat contains 8–20% proteins which include albumins, globulins, gliadins and glutenins. Glutenins are the composite of gluten and glutelins that are stored together with starch in the endosperm. Gluten is found in wheat, barley, rye, oat and related species and is known for its viscoelastic properties. They trigger food-sensitive enteropathies in humans: Celiac Disease (CD), Irritable Bowel Syndrome (IBS), wheat allergy, non-celiac gluten sensitivity (NCGS), and so forth, due to inability to digest gluten. Presently, the only effective treatment is strict gluten-free diet, life-long. However, probiotics are used in varying degrees for treating such disorders. The present study highlights the use of protease producing probiotic strains to degrade gluten proteins thus decreasing its toxicity. From the 25 isolates screened, six (Ich1, Ich3, Ic1, Ic3, Ic4, and Lactobacillus plantarum) showed significant gluten and standard gliadin degradation and Ich1 showed the highest gluten and standard gliadin degradation by 85.32 and 70.0% respectively. This could be attributed to their high protease activity, and these isolates clearly demand further studies on their potentiality as novel dietary supplement for therapeutic application. Novelty Impact Statement In the present investigation, highest gluten degradation of 85.32 and 82.12% were observed with ICh1 and IC4 respectively, which was significant than that of Lactobacillus plantarum. It was found from the present investigation that protease producing probiotic isolates were capable of degrading wheat gluten which was directly proportional to the amount of enzyme.