Studies on the mechanism of destruction of the toxic action of wheat gluten in coeliac disease by crude papain

Abstract

EDITORIAL SYNOPSIS The toxic action of wheat gluten on two patients was eliminated after predigestion of gluten by crude papain. This change is thought to be due to an enzyme which liberates ammonia from gluten. It is not thought that this particular mechanism operates in the normal intestinal cell but it is envisaged that one of the peptide bonds of the coeliac active constituent (possibly a N-glutaminyl peptide) is normally split by a specific intestinal peptidase which is defective in coeliac patients.Previous authors have shown that the harmful action of dietary wheat gluten in coeliac disease or non-tropical sprue is not eliminated by predigesting the gluten with either pancreatin or pepsin or trypsin

Nutritional and Phyto-Therapeutic Potential of Papaya (Carica Papaya Linn.): An Overview

“…Thus, it can be prescribed for dyspeptic and celiac disease patients, who cannot digest wheat protein gliadin but can tolerate it if it is treated with crude papain. The pure papain activity was rather low, in agreement with the work carried out by Messer et al [67] They reported that crude papain is responsible for giladin detoxification. [68] Additionally, utilization of crude papain for hydrolyzing gluten is an appropriate and economic approach.…”

Circulating antibodies to wheat gliadin fractions in coeliac disease

“…The low haemagglutination titres obtained against fractions rich in pyrrolidone carboxylyl peptides are consistent with the findings of Sela (1969) on the importance of the N-terminal amino group in humoral antibody production. Messer, Anderson, and Hubbard (1964) thought ring closure of N-glutaminyl peptides could be a possible mechanism explaining the detoxification of gluten by digestion with crude papain. The low titres against partially deamidated digests parallel the observed effects of deamidation on toxicity (Weijers, van de Kamer, and Dicke, 1957), though the process used is also known to cause ring closure of Nglutaminyl peptides.…”

Detoxification of Gluten by Means of Enzymatic Treatment

“…However, no details of the experimental design were given. Similarly, the digestion of gluten with crude papain resulted in a nontoxic product, whereas pure crystalline papain did not show any effect (23). After that time, there was a long break in studying enzymatic systems for the detoxification of gluten.…”