Properties and applications of microbial transglutaminase.

  • Jones M
  • Ganopolsky J
  • Labbé A
 et al. 
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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 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.

Author-supplied keywords

  • animals
  • anti infective agents
  • anti infective agents administration & dosage
  • anti infective agents metabolism
  • anti infective agents pharmacology
  • bacteria
  • bacteria drug effects
  • bacteria metabolism
  • drug delivery systems
  • eukaryotic cells
  • eukaryotic cells metabolism
  • fungi
  • fungi drug effects
  • humans
  • nitric oxide
  • nitric oxide administration & dosage
  • nitric oxide metabolism
  • nitric oxide pharmacology

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  • PMID: 20680266

Authors

  • Mitchell Lawrence Jones

  • Jorge Gabriel Ganopolsky

  • Alain Labbé

  • Christopher Wahl

  • Satya Prakash

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