MICROBIAL TRANSGLUTAMINASE - A REVIEW OF ITS PRODUCTION AND APPLICATION IN FOOD-PROCESSING

Transglutaminase (EC 2.3.2.13) catalyses an acyl-transfer reaction in which the gamma-carboxamide groups of peptide-bound glutaminyl residue s are the acyl donors. The enzyme catalyses in vitro cross-linking in whey proteins, soya proteins, wheat proteins, beef myosin, casein and crude actomyosin refined from mechanically deboned poultry meat. In re cent years, on the basis of the enzyme's reaction to gelatinize variou s food proteins through the formation of cross-links, this enzyme has been used in attempts to improve the functional properties of foods. U p to now, commercial transglutaminase has been merely obtained from an imal tissues. The complicated separation and purification procedure re sults in an extremely high price for the enzyme, which hampers a wide application in food processing. Recently studies on the production of transglutaminase by microorganisms have been started. The enzyme obtai ned from microbial fermentation has been applied in the treatment of f ood of different origins. Food treated with microbial transglutaminase appeared to have an improved flavour, appearance and texture. In addi tion, this enzyme can increase shelf-life and reduce allergenicity of certain foods. This paper gives an overview of the development of micr obial transglutaminase production, including fermentation and down-str eam processing, as well as examples of how to use this valuable enzyme in processing foods of meat, fish and plant origin.