Microbial Transglutaminase is Beneficial to Food Industries but a Caveat to Public Health

Aaron Lerner ,Torsten Matthias

doi:10.20900/mo.20190001

Abstract

Microbial transglutaminase (mTG) is a survival factor for bacteria that is heavily used as a protein glue in the processed food industries. Despite the manufacturersâ claims for it safe usage, scientific observations are accumulating for its unwanted effects on human health. The enzyme can cross link proteins, imitating its family member, tissue transglutaminase, the autoantigen of celiac disease. Its gliadin cross-linked complexes are immunogenic in celiac disease. In the intestinal lumen, mTG exerts anti protease activity and forms resistant isopeptide bonds, it is anti-phagocytic, thus suppressing luminal protective pathways. It increases intestinal permeability, is trans-epithelialy transported and faces the enteric mucosal immune cells. Finally, mTG-containing products can react as emulsifiers and mucolytic agents thus compromising barriersâ integrities. The present review summarizes and updates on the potential detrimental effects of mTG, aiming to protect the public from the enzymeâs unwanted effects.

Highlights

Transglutaminases (TGs) (EC 2.3.2.13), i.e., protein-glutamine γ-glutamyltransferase, are multi-functional, pleiotropic enzymes, expressed ubiquitously and extensively in living organisms
The present review will concentrate on the prokaryotic TGs, the microbial TG, highlighting its massive uses in the processed food industries, as a food additive. It appears that Microbial transglutaminase (mTG), a bacterial survival factor, is beneficial for the food industry, but, its public safety is under investigation where various potential detrimental effects were recently described or suggested
Being a gluten-based peptide, mTG cross-linked gliadin can duplicate the effect on the tight junction

Summary

Introduction

Transglutaminases (TGs) (EC 2.3.2.13), i.e., protein-glutamine γ-glutamyltransferase, are multi-functional, pleiotropic enzymes, expressed ubiquitously and extensively in living organisms. It appears that mTG, a bacterial survival factor, is beneficial for the food industry, but, its public safety is under investigation where various potential detrimental effects were recently described or suggested. TTG is endogenous, while mTG is exogenous, a common enzyme of the prokaryotic kingdom, considered as an environmental factor that potentially can affect human health, as detailed below. Considering its protein modifying abilities, exerting deamidation and transamidation, it imitates functionally the endogenous tTG [2,3,6,13].

Results

Conclusion