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

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      Folia Microbiologica
      Springer Netherlands

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          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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          Properties and applications of microbial transglutaminase.

          Some properties and applications of the transglutaminase (TGase) referred to as microbial TGase (MTGase), derived from a variant of Streptomyces mobaraensis (formerly classified as Streptoverticillium mobaraense), are described. MTGase cross-linked most food proteins, such as caseins, soybean globulins, gluten, actin, myosins, and egg proteins, as efficiently as mammalian TGases by forming an epsilon-(gamma-glutamyl)lysine bond. However, unlike many other TGases, MTGase is calcium-independent and has a relatively low molecular weight. Both of these properties are of advantage in industrial applications; a number of studies have illustrated the potential of MTGase in food processing and other areas. The crystal structure of MTGase has been solved. It provides basic structural information on the MTGase and accounts well for its characteristics. Moreover, an efficient method for producing extracellular MTGase has been established using Corynebacterium glutamicum. MTGase may be expected to find many uses in both food and non-food applications. Copyright 2004 Springer-Verlag
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            Transglutaminase and its use for food processing

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              Network Formation in Gluten-Free Bread with Application of Transglutaminase

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                Author and article information

                Contributors
                +48-22-6063680 , +48-22-8490426 , marek-kieliszek@wp.pl
                Journal
                Folia Microbiol (Praha)
                Folia Microbiol. (Praha)
                Folia Microbiologica
                Springer Netherlands (Dordrecht )
                0015-5632
                1874-9356
                8 November 2013
                8 November 2013
                2014
                : 59
                : 241-250
                Affiliations
                [ ]Department of Microbiology, Institute of Agricultural and Food Biotechnology, Rakowiecka, 36 St., 02-532 Warsaw, Poland
                [ ]Department of Biotechnology, Microbiology and Food Evaluation, Faculty of Food Sciences, Warsaw University of Life Sciences - SGGW, Nowoursynowska 159 C St., 02-776 Warsaw, Poland
                Article
                287
                10.1007/s12223-013-0287-x
                3971462
                24198201
                e57eebcd-5cd1-4544-8d3f-8e96317d1cfe
                © The Author(s) 2013

                Open Access This article is distributed under the terms of the Creative Commons Attribution License which permits any use, distribution, and reproduction in any medium, provided the original author(s) and the source are credited.

                History
                : 26 March 2013
                : 14 October 2013
                Categories
                Article
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                © Institute of Microbiology, Academy of Sciences of the Czech Republic, v.v.i. 2014

                Microbiology & Virology
                Microbiology & Virology

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