Transglutaminase: Fundamentals and Applications

By Yi Zhang

Transglutaminase: Fundamentals and Applications, a new volume in the Foundations and Frontiers in Enzymology series, stands as a comprehensive resource on this increasingly important class of enzymes. Following an introduction to the field from the Editors, international experts discuss basic biology and structure – function relationships of transglutaminases, ongoing fundamental research, as well as new application areas, including food processing, material synthesis, biomedicine and disease treatment, and biotechnology. Approaches for sourcing transglutaminases from animals, plants, and microorganisms are considered in-depth, followed by chapters on applied uses in biomedicine, skin and bone biology and medicine, drug development, tissue engineering, seafood bioprocessing, dairy bioprocessing, synthesis of materials and polymers, and as an immobilization agent. Research protocols are also provided, including research rationale, design, substrates, assays and microassay steps for studying transglutaminases.

• Brings together basic knowledge and applied research on transglutaminase biology
• Considers a range of application areas, from biomedicine to drug development, tissue engineering, food processing, and materials synthesis
• Includes instructive protocols for basic and applied transglutaminase research
• Features chapter contributions from global leading experts in the field, across disciplines and applications

• Language: English
• Publisher: Academic Press
• Release date: Feb 26, 2024
• ISBN: 9780443191695

Book preview

1: Transglutaminases from microorganisms

Limin Wang ¹ , and Yi Wang ¹ , ²       ¹CAS Key Laboratory of Microbial Physiological & Metabolic Engineering, State Key Laboratory of Mycology, Institute of Microbiology, Chinese Academy of Sciences, Beijing, China      ²University of Chinese Academy of Sciences, Beijing, China

Abstract

Transglutaminase (TGase) catalyzes acyl-transfer reactions between proteins. It has been widely used to modify the functional properties of proteins in the food industry. TGases are widely distributed in nature, existing in vertebrates, invertebrates, microorganisms, and plants. The extremely high costs and complexity of isolating TGase from animal tissues have prompted scientists to search for new sources of this enzyme. Microbial TGase (MTGase) could be obtained by conventional fermentation, which provides an easy-to-use method for the green production of TGase. This chapter points to the enzymological characteristics of TGase from various microbial sources. The enzymatic properties of MTGase, MTGase biosynthesis procedures, and the potential of genetic engineering for MTGase production are also highlighted.

Keywords

Biosynthesis; Enzymatic property; Genetic engineering; Microorganisms; Transglutaminase

1. Introduction

Transglutaminase (TGase, EC 2.3.2.13) is a member of the transferase family, which catalyzes the acyl transfer reaction between γ-carboxamide of glutaminyl residues as acyl donors and primary amines as acyl acceptors (Santhi et al., 2017). It is recognized as GRAS (Generally Recognized as Safe), a safe substance for human ingestion (Gaspar and de Góes-Favoni, 2015). TGase has been widely used for enhancing the functions and textures of dairy, meat, fish, and soy products (Yang and Zhang, 2019). Native TGase was first found in animal tissues, and extraction from animal tissues was the commercial way until the end of the 18th century. In addition to the high cost of animal-derived TGase, there are two reasons why animal-derived TGase is rarely used nowadays. One reason is that animal-derived TGase is a Ca²+-dependent protein. Ca²+ may destabilize some food proteins, such as caseins and soy proteins, which limits their application in the food industry (Cui et al., 2007). The second reason is that TGase from animals causes the precipitation of casein, soy globulin, myoglobin, and other substances in the organism, which threatens the safety of the organism and triggers a series of adverse reactions, such as metabolic disorders (Martins et al., 2014). This phenomenon gradually promotes the development of TGases from other sources. Nowadays, TGases have been found in mammalian tissues, microbial cells, and plant tissues (Kieliszek and Misiewicz, 2014). Microbial TGase (MTGase) has been found in many bacteria, including Streptomyces mobaraense, Streptomyces cinnamoneum, Streptomyces ladakanum, S. hygroscopicus, Bacillus circulans, and Bacillus subtilis (Ehab and Gavin, 2017), and the cell wall of fungi (Wang et al., 2018). Compared with TGase from animals and plants, MTGase is a Ca²+-independent enzyme with broad applications in the food industry. MTGase could be produced by conventional fermentation, thus, TGase of microbial origin became the one of choice for commercial use (Kieliszek and Misiewicz, 2014). In this chapter, we will focus on the advances in TGase from microorganisms and biotechnological routes for the active and inactive production of MTGase. The enzymatic properties of MTGase and MTGase biosynthesis procedure will also be reviewed. The drawbacks and improvements in the production of TGase via conventional fermentation and biotechnological routes will be