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Review
. 2014 May;59(3):241-50.
doi: 10.1007/s12223-013-0287-x. Epub 2013 Nov 8.

Microbial transglutaminase and its application in the food industry. A review

Marek Kieliszek  1 , Anna Misiewicz
Affiliations
Review

Microbial transglutaminase and its application in the food industry. A review

Marek Kieliszek et al. Folia Microbiol (Praha). 2014 May.

Abstract

The extremely high costs of manufacturing transglutaminase from animal origin (EC 2.3.2.13) have prompted scientists to search for new sources of this enzyme. Interdisciplinary efforts have been aimed at producing enzymes synthesised by microorganisms which may have a wider scope of use. Transglutaminase is an enzyme that catalyses the formation of isopeptide bonds between proteins. Its cross-linking property is widely used in various processes: to manufacture cheese and other dairy products, in meat processing, to produce edible films and to manufacture bakery products. Transglutaminase has considerable potential to improve the firmness, viscosity, elasticity and water-binding capacity of food products. In 1989, microbial transglutaminase was isolated from Streptoverticillium sp. Its characterisation indicated that this isoform could be extremely useful as a biotechnological tool in the food industry. Currently, enzymatic preparations are used in almost all industrial branches because of their wide variety and low costs associated with their biotechnical production processes. This paper presents an overview of the literature addressing the characteristics and applications of transglutaminase.

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Figures

Fig. 1
Fig. 1
The reactions catalysed by transglutaminase included. a acyl-transfer reaction; b cross-linking reaction between Gln and Lys residues of proteins or peptides. c deamidation
Fig. 2
Fig. 2
Process chart of transglutaminase production
Fig. 3
Fig. 3
Possible applications of microbial transglutaminase
See this image and copyright information in PMC

References

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