Transglutaminase Catalyzed Reactions: Impact on Food Applications

Abstract

Transglutaminases can perform various reactions that are based on cross-linking, acyl-transfer and deamidation. These enzymes are found in many different organisms where they have very specific roles. The basic reaction mechanism of these transglutaminases is similar. The reactions catalyzed by transglutaminases have proven to be useful in production of different kinds of protein ingredients and food products. In this review, we will show important aspects of transglutaminase cross-linking in respect to substrate specificity, accessibility of proteins, regulation and differences in reactions and safety. These aspects will be viewed in respect to food applications

The Properties of Edible Film Derived From Bovine Split Hide Gelatin With Isolated Soy Protein Using Various Levels of Glycerol in the Presence of Transglutaminase

“…Chambi and Grosso (2006) was able to create an edible film of a combination of B-type bovine gelatin with casein through an enzymatic process.The enzyme that was often used as a crosslinked agent among the two proteins was transglutaminase enzyme (TGse, proteinglutamine c-glutamyl transferase, EC 2.3.2.13) catalyzed the reaction of acyl transfer between the γ-glutamine residues carboxiamide group (acyl donor) and the eamino lysine residues (acyl acceptor), resulting in the formation of (e-γ -glutamyl) lysine intra-and intermolecular cross-linked protein (De Jong and Koppelman, 2002). The formation of crosslinking did not reduce the nutritional quality of the food as lysine residues remain available for digestion (Yokohama et al, 2004).…”

Structured biopolymer-based delivery systems for encapsulation, protection, and release of lipophilic compounds

“…Gelatin can be gelled by cooling a biopolymer solution below the helixecoil transition temperature to promote the formation of helices and hydrogen bond cross-links (Izmailova et al, 2004). Enzymes such as transglutaminase can also be used to form covalent cross-links between amino acids on various protein substrates (DeJong & Koppelman, 2002), which has recently been used to form biopolymer delivery systems for lipophilic components (Huppertz & de Kruif, 2008;Song, Zhang, Shi, & Li, 2010).…”

Protein-Based Edible Films: Characteristics and Improvement of Properties

“…However, transglutaminase is a kind of enzyme which can catalyze the covalent cross linking reactions between proteins to form high molecular weight (MW) biopolymers. De Jong & Koppelman (2002) reported that transglutaminase catalyzes acyltransfer reactions between λ-carboxyamide groups of glutamine residues (acyl donor) and ε-amino groups of lysine residues (acyl acceptor), resulting in the formation of ε-(λ-glutaminyl) lysine intra and intermolecular cross-linked proteins. The reaction catalyzed of glutamyltransferases is shown in Figure 2 (Yee et al, 1994) Polymerization using transglutaminase has been investigated with various protein sources including casein, soy proteins and gelatin, where different responses in gel strength were dependent on the reaction conditions and on the different protein sources (Sakamoto et al, 1994).…”