Effects of transglutaminase on health properties of food products

Nowadays, food manufacturers try to develop new products with unique functional characteristics; however, these products have not always been to the benefit of the consumer and in some cases have led to consumer's health problems. The use of transglutaminase (TG) in the food industry is very common. Transglutaminase catalyzes covalent bond between lysine and glutamine in peptides and protein to achieve a more stable, rigid and complex product. From the health point of view, TG can reduce allergy, control energy intake from foods and act as mediator in wound healing. Besides all these benefits, evidences have suggested that transglutaminase (mTG) action in food products might cause autoantigen in celiac disease (CD) population. Microbial transglutaminase cross-linked gluten may be hazardous for CD since the enzymes can deamidate gluten and thus, mimic endogenous tissue transglutaminase (tTG). On the other hand, numerous studies indicated that transglutaminase is responsible for some neurodegenerative diseases such as Alzheimer disease and Huntington disease (HD). In the present article, recent achievements on health aspects of transglutaminase in food products are reviewed.