Biotechnological Applications of Transglutaminases

Abstract

In nature, transglutaminases catalyze the formation of amide bonds between proteins to form insoluble protein aggregates. This specific function has long been exploited in the food and textile industries as a protein cross-linking agent to alter the texture of meat, wool, and leather. In recent years, biotechnological applications of transglutaminases have come to light in areas ranging from material sciences to medicine. There has also been a substantial effort to further investigate the fundamentals of transglutaminases, as many of their characteristics that remain poorly understood. Those studies also work towards the goal of developing transglutaminases as more efficient catalysts. Progress in this area includes structural information and novel chemical and biological assays. Here, we review recent achievements in this area in order to illustrate the versatility of transglutaminases.

The LQSP tetrapeptide is a new highly efficient substrate of microbial transglutaminase for the site‐specific derivatization of peptides and proteins

“…The LQSP tetrapeptide is a new highly efficient substrate of microbial transglutaminase for the site-specific derivatization of peptides and proteins Andrea Caporale 1 , Fabio Selis 2 , Annamaria Sandomenico 1,3 , Gloria S. Jotti 4 , Giancarlo Tonon 2 and Menotti Ruvo 1,3 genic, and more resistant to proteolytic degradation [5]. An extremely valuable approach is the site-specific modification of biotherapeutics with poly(ethyleneglycol) (PEG), a nontoxic and very effective reagent far improving pharmacokinetic and pharmacodynamic properties when molecular masses are below 1000 Da [6].…”

“…Calcium-independent TGases have also been identified, including one identified from microbial sources (M-TGase). M-TGase is far more stable and is commonly employed as a tool in the food industry to catalyze the cross-linking of meat, soy, and wheat proteins to improve their texture and tensile properties [3]. Reactions by M-TGase lead to post-translational modifications of proteins through the formation of either intra-and intermolecular isopeptide bonds or the covalent attachment of polyamines and primary alkylamines, such as putrescine, spermidine, and spermine, generating different monosubstituted γ-modified glutamines [4].…”

Transglutaminases: recent achievements and new sources

“…The cysteine and the histidine residues are principally involved in the acyl-transfer reaction, where the aspartic acid residue hydrogen bonds with the histidine, maintaining a catalytically competent orientation. The crystal structure of MTG revealed that this triad is not conserved; rather, it was proposed that MTG uses a cysteine protease-like mechanism in which Asp plays the role of the histidine residue in factor XIII-like TGases (Rachel and Pelletier 2013) (Fig. 2).…”

Recent developments in biocatalysis beyond the laboratory

“…Oftentimes, these interand intra-crosslinking reactions alter numerous functional characteristics including viscosity, gelation, solubility, heat stability, and water holding capacity of a given protein system and therefore the final product (Ramos and Malcata 2011). In this respect, over the past few years microbial transglutaminases (MTGs) have attracted interest for these food modification applications (de Goes-Favoni and Bueno 2014;Kieliszek and Misiewicz 2014;Martins et al 2014;Rachel and Pelletier 2013).…”