Article | REF: F4750 V1

Transglutaminase - Properties and application in the Food Industry

Author: Abdul-Hamid Klandar

Publication date: December 10, 2025 | Lire en français

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    Overview

    ABSTRACT

    Transglutaminase is an enzyme that catalyzes the formation of irreversible isopeptide bonds between proteins or peptides for improving the firmness, viscosity, elasticity, and water-holding capacity of food products. This enzyme was produced and isolated by traditional fermentation from Streptoverticillium mobaraensis in 1989 (Ajinomoto, Japan). Its crosslinking property is widely used in many industries including food manufacturing. This paper presents an overview of the works dealing with applications of transglutaminase in the manufacturing of dairy products, meat and processed seafood products, bakery products, and plant-based products.

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    AUTHOR

    • Abdul-Hamid Klandar: Head of the Laboratory for Enzymatic Application Development in Dairy Products and Analogues, Paris, France

     INTRODUCTION

    Enzymes were used long before the development of enzyme production technologies using fermentation with microorganisms. However, with the rise of advanced bioprocesses using recombinant DNA technology, enzymes are purified and produced on a larger scale, which has enabled their use and applications in various food industries. They are agents that play an important role in the physical and physicochemical properties of different foods.

    The development of protein engineering with directed evolution at the active site has led to the creation of new enzymes with improved activities. Among industrial enzymes, the most widely used are hydrolases and glucidases. Hydrolases, such as lipases and proteases, are the dominant type in many food industries, mainly dairy. Glucidases include amylases and cellulases and are also widely used.

    The use of enzymes to modify proteins offers numerous advantages due to the specific nature of the reactions and the low frequency of side reactions, without the need for high pressure and high temperature conditions. These advantages make the use of enzymes effective, particularly in the food industry. In terms of the application of hydrolases in industry, proteases have been the main enzymes used for food proteins until now. With the emergence of the enzyme transglutaminase (EC 2.3.2.13), involved in protein cross-linking, the technological possibilities for protein modification have expanded considerably. It belongs to the transferase family, which is widespread in nature.

    Transglutaminase is present in the blood of mammals, birds, poultry, fish, and crustaceans, as well as in plants such as peas, sunflowers, Jerusalem artichokes, and fodder beets. Mammalian transglutaminases are dependent on ionic calcium. In the early 1990s, a new transglutaminase produced by a microorganism was discovered for the first time. In the 1990s, the first microbial transglutaminase derived from the S-8112 strain of Streptoverticillium mobaraense (Ajinomoto, Japan) was commercialized. It has been used in deli meats, dairy products, baked goods, and vegan products.

    This article focuses on the use of transglutaminase in many branches of the food industry. From a techno-economic point of view, protein resources become less recoverable during the processing of ingredients or food products. As a result, transglutaminase could be a technological aid to improve this recovery without compromising the quality of the finished products. The article briefly describes the enzymatic properties of transglutaminase, its origin, and its detailed applications in the dairy, meat and seafood, bakery, and reconstituted vegetable protein substitute industries. A presentation of the regulatory aspects of this enzyme is also included,...

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    KEYWORDS

    transglutaminase   |   protein cross-linking   |   streptoverticillium mobaraensis


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