Transglutaminases: part I—origins, sources, and biotechnological characteristics

Abstract

The transglutaminases form a large family of intracellular and extracellular enzymes that catalyze cross-links between protein molecules. Transglutaminases crosslinking properties are widely applied to various industrial processes, to improve the firmness, viscosity, elasticity, and water-holding capacity of products in the food and pharmaceutical industries. However, the extremely high costs of obtaining transglutaminases from animal sources have prompted scientists to search for new sources of these enzymes. Therefore, research has been focused on producing transglutaminases by microorganisms, which may present wider scope of use, based on enzyme-specific characteristics. In this review, we present an overview of the literature addressing the origins, types, reactions, and general characterizations of this important enzyme family. A second review will deal with transglutaminases applications in the area of food industry, medicine, pharmaceuticals and biomaterials, as well as applications in the textile and leather industries.

Intein-mediated intracellular production of active microbial transglutaminase in Corynebacterium glutamicum

“…The pro-peptide of zymogen was presumed to assist the zymogen folding but also to inhibit the toxicity of mature peptide [1,42]. Without the coexpression of pro-peptide, mTGase was constantly expressed as inclusion bodies in E. coli [43,44] and C. glutamicum (Additional le 1: Figure S1), suggesting that the pro-peptide of mTGase was essential for mTGase precursor folding.…”

“…Transglutaminase (EC 2.3.2.13, TGase) catalyzes the acyl-transfer between glutamine residues and varieties of primary amines and results in the crosslinking of proteins [1,2]. Owing to the crosslinking properties, TGase shows great potential for application in the food, pharmacological and biotechnological industries [3][4][5].…”

Enzymatic Methods for the Site-Specific Radiolabeling of Targeting Proteins

“…Transglutaminases (TGase; EC 2.3.2.13) are enzymes that catalyze the cross-linking between ε-amino group of Lys residues and γ-carboxamide group of Gln residues of proteins through the formation of ε-(γ-glutamyl)lysine isopeptide bonds, which are stable and protease resistant, and the release of ammonia (Figure 2A) [28]. TGases are a large family of enzymes detected in several organisms, including mammals, invertebrates, plants, and microorganisms [29]. In mammals, TGases are involved in important physiological functions, such as blood coagulation and keratogenesis and pathological processes as cancer and tissue fibrosis [30].…”

“…The TGase reaction is nowadays also widely exploited for the production of protein derivatives, in tissue engineering and in food and leather processing [31][32][33][34][35]. For industrial applications and protein conjugation, bacterial TGases are preferred which show little sequence similarity with mammalian TGases [29,36]. In particular, a TGase isolated from Streptomyces mobaraensis called microbial transglutaminase (mTG) offers several advantages in respect to mammalian TGases as calcium-independence, nearly half molecular mass, a lower substrate specificity, a lower deamidation activity, and availability in large quantities and with lower costs [37,38].…”

Enzyme‐catalysed polymer cross‐linking: Biocatalytic tools for chemical biology, materials science and beyond

“…Recently, Duarte et al have published two reviews examining the origins and applications of transglutaminases where they discuss in depth their biological functions, as well as the optimal conditions for these enzymes from various organisms involved in many of the applications listed in Table 2. [32] 3 | SORTASE-MORE THAN JUST ANOTHER BRICK IN THE (CELL) WALL group present on a secondary substrate. [33] The best studied sortases are those of the sortase A (SrtA) class, the so called 'housekeeping'…”