2 Kallang Avenue #07-18
CT HUB, 339407
The gelatin system of yogurt is maintained by very weak non-covalent bonds, mainly hydrogen bonds. This gelatin system is very fragile,so the tissue state can be easily destroyed and whey precipitation during mixing, storage and transportation, thus losing commercial value. In term of casein of cow's milk, transglutaminase enzyme can achieve the purpose of milk modification, mainly in improving the textural gel strength of yogurt, enhancing the water and gelation, and improving thermal stability. Currently its application scenario mainly focus on mixing yogurt, cheese, raw milk, etc.
TG Prolink D Series catalyzes the acyl transfer reaction between the γ-carboxamido group of glutamine residues and the ε-amino group of lysine residues in milk protein polypeptide chains to form ε-(γ-glutamine) lysine isopeptide bonds, resulting in intramolecular and intermolecular covalent cross-linking of proteins to form a more dense reticulation mechanism. Through these reactions, the functional properties of various proteins, such as nutritional value, textural structure, taste and storage life, can be improved.
After the cow's milk is treated by transglutaminase enzymes, the gelatin strength produced by the yogurt produces is significantly improved than unbroken samples. The whey precipitation is also significantly reduced. The stability of the yogurt is better, thereby reducing the production capital, increasing the performance rate, and extending the shelf period. What's more, the texture and stability of the yogurt produced by low-fat and low-protein raw materials are similar to the yogurt produced by normal milk. The whey protein of TG-treated milk was also able to be attached to the network structure by TG, increasing the protein content. Since TG enzyme can introduce lysine, its amino acid content is also increased, so it can significantly improve the functional properties of the protein.
In cheese processing, it is assumed that the addition of a mixture of transglutaminase enzyme and glutathione to unheated or pasteurized skim milk can significantly increase the efficiency of TG utilization and reduce the amount of TG used. The yield of cheese was greatly increased as the proteins in whey were also linked by TG into the gel network construct. It is argued that the participation of a mixture of TG and glutathione is followed by a significant improvement in the functional properties of the protein, this function is used more widely in soft and semi-hard cheeses.
As food-grade dairy additives, transglutaminase enzymes are important in improving the heat stability of milk and in preventing caking and hardening of milk powder. But market prospects need to be debated.
Transglutaminase enzyme (TGase) catalyzes the formation of an ε-(Υ-glutamyl) lysyl covalent bond between protein molecules, which is difficult to break under normal non-enzymatic catalytic conditions, and can make protein molecules more closely together, which is an enzyme that can catalyze intra- and intermolecular covalent cross-linking of protein polypeptides, and this cross-linking can improve the structure and function of proteins. It has significant effects on protein properties such as: foaming, emulsification, stability, thermal stability, water retention and gelation ability, etc. It can make the meat protein of the meat block itself naturally cross-linked, and bond protein molecules together. It is applied to beef, pork, chicken and other meat products, which not only can improve its taste, flavor, tissue structure and nutrition, but also improve the added value of the product.