Abstract
Microbial transglutaminase (mTG) is a heavily used food additive and its industrial transamidated complexes usage is rising rapidly. It was classified as a processing aid and was granted the GRAS (generally recognized as safe) definition, thus escaping full and thorough toxic and safety evaluations. Despite the manufacturers claims, mTG or its cross-linked compounds are immunogenic, pathogenic, proinflammatory, allergenic and toxic, and pose a risk to public health. The enzyme is a member of the transglutaminase family and imitates the posttranslational modification of gluten, by the tissue transglutaminase, which is the autoantigen of celiac disease. The deamidated and transamidated gliadin peptides lose their tolerance and induce the gluten enteropathy. Microbial transglutaminase and its complexes increase intestinal permeability, suppresses enteric protective pathways, enhances microbial growth and gliadin peptide’s epithelial uptake and can transcytose intra-enterocytically to face the sub-epithelial immune cells. The present review updates on the potentially detrimental side effects of mTG, aiming to interest the scientific community, induce food regulatory authorities’ debates on its safety, and protect the public from the mTG unwanted effects.
Highlights
The transglutaminase secreted by bacteria is called microbial transglutaminase.Evolutionally, it is an important survival factor for prokaryotes like bacteria, fungi and actinomycetes
Apical-basal transfer of various gliadin peptides is assisted by secretory IgA and apical transferrin receptor when tissue transglutaminase (tTG) is applied on epithelial cells [77]
Microbial transglutaminase is used as glue to cross-link proteins and other molecules during food processing
Summary
The transglutaminase secreted by bacteria is called microbial transglutaminase (mTG). Many studies have been conducted to find microbial sources capable of secreting the enzyme due to its outstanding capacity to cross-link proteins or peptide [1,2,3]. Having group of γ-carboxamides of glutamine residues (acyl residue donor) and the first-order εthe capacity ofdifferent post translation modification of proteins, it can deamidate or cross-link amine groups of compounds, like proteins or peptides substrates [17,18]. Having the capacity translation modification proteins, can deamidate cross-[8] In this regard, mTG is heavily consumed in a plethora of processed food manufacturers. It improves texture, preservability and improves texproduct hardness, improves protein film appearance and stability and even decreases ture and quality of liquid milk and dairy products. The estimated mTG doses to restructure 1 kg of food products is in the range of about 50–100 mg of the enzyme [3,9,12,28]
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