Ecology, Environment and Conservation Paper

Vol. 19, Issue 01, 2013; Page No.(57-60)

MICROBIAL TRANSGLUTAMINASES AND THEIR APPLICATIONS

S. Vijay Kumar Reddy, Rajkumar Ratnakumar Singh, Faisal Rashid Sofi and G. Vidya Sagar Reddy

Abstract

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 ε-(γ 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 nonfood applications.

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