It is no secret that,if used properly, the application of the transglutaminase enzyme (TG) in bakery products can promote great improvement in dough texture, volume, and gas retention, even when combined with other enzymes.
Transglutaminases (EC 18.104.22.168, γ-glutamyl-peptide, amine-γ-glutamyl-transferase) belong to the group of acyltransferases, which catalyze acyl-transfer reactions between a γ-carboxyamine, group of a peptide – or protein-bond glutamyl residue and a primary amino group of various substrates including the ε-amino group of lysine or lysyl residues in proteins, resulting in polymerization or amine incorporation.
The result cross-link is called a ε-(γ-glutamyl)lysine isopeptide bond). During the reaction a single molecule of ammonia is generated per cross-link. In case the amine substrates are not available as acyl acceptors, it is possible for TG to catalyse deamination of glutamyl residues using water as an acyl acceptor. In contrast to their limited glutamine (an acyl donor) substrate specificity, TG possesses a wide specificity for the acyl acceptor substrates
By using an innovative technology which concentrates and encapsulates the protein this issue can be avoided without affecting performance of the transglutaminase enzyme in industrial processing or long storage of the dough improver.
New trials with this new stable TG generation showed best improved effects.