Microbial transglutaminase and its application in the food industry. A review
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- 作者：Marek Kieliszek (1) (2)
Anna Misiewicz (1) - 刊名：Folia Microbiologica
- 出版年：2014
- 出版时间：May 2014
- 年：2014
- 卷：59
- 期：3
- 页码：241-250
- 全文大小：573 KB
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Anna Misiewicz (1)
1. Department of Microbiology, Institute of Agricultural and Food Biotechnology, Rakowiecka, 36聽St., 02-532, Warsaw, Poland
2. 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 - ISSN：1874-9356
文摘
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.