Properties and applications of microbial transglutaminase

@article{Yokoyama2003PropertiesAA,
  title={Properties and applications of microbial transglutaminase},
  author={Kei-ichi Yokoyama and Noriki Nio and Yoshimi Kikuchi},
  journal={Applied Microbiology and Biotechnology},
  year={2003},
  volume={64},
  pages={447-454}
}
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… Expand
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References

SHOWING 1-10 OF 62 REFERENCES
NMR-based screening method for transglutaminases: rapid analysis of their substrate specificities and reaction rates.
TLDR
An NMR-based method using the enzymatic labeling technique (ELT) for simultaneous analysis of the substrate specificities and reaction rates of TGases is developed and has shown that MTG is superior for industrial use because of its lower substrate specificity compared with those of guinea pig liver transglutaminase (GTG) and red sea bream liver transGLutaminases (FTG). Expand
Microbial transglutaminase—a review of its production and application in food processing
TLDR
An overview of the development of microbial transglutaminase production, including fermentation and down-stream processing, as well as examples of how to use this valuable enzyme in processing foods of meat, fish and plant origin are given. Expand
Primary structure of microbial transglutaminase from Streptoverticillium sp. strain s-8112.
TLDR
The results suggest that this microbial protein evolved by a different pathway from that of mammalian TGases and acquired acyl transfer activity during the evolutional process. Expand
Purification and Characteristics of a Novel Transglutaminase Derived from Microorganisms
A microorganism producing transglutaminase was screened as an indication of hydroxamate- forming activity. The microbial transglutaminase was purified from the culture filtrate of the strain, S-Expand
Bacterial pro-transglutaminase from Streptoverticillium mobaraense--purification, characterisation and sequence of the zymogen.
TLDR
It could be shown that the micro-organism produces a protease which cleaves pro-transglutaminase at the C-side of Pro45, and Rapid transformation of the mature enzyme also occurs by addition of other proteases. Expand
Chemical synthesis of the gene for microbial transglutaminase from Streptoverticillium and its expression in Escherichia coli.
TLDR
The gene coding for microbial transglutaminase from Streptoverticillium, which consists of 331 amino acids, was chemically synthesized and was identical with native TGase in size and in immunological properties, though the enzyme activity was low. Expand
Overproduction of Microbial Transglutaminase in Escherichia coli, In Vitro Refolding, and Characterization of the Refolded Form
TLDR
Results indicated that recombinant MTG could be produced efficiently in E. coli, and showed activity equivalent to that of native MTG. Expand
Crystal Structure of Microbial Transglutaminase fromStreptoverticillium mobaraense *
TLDR
The structure accounts well for the catalytic mechanism, in which Asp255 is considered to be enzymatically essential, as well as for the causes of the higher reaction rate, the broader substrate specificity, and the lower deamidation activity of this enzyme. Expand
Amine-binding capacities of food proteins in transglutaminase reaction and digestibility of wheat gliadin with ε-attached lysine
Several food proteins were examined for their capacity as substrate in transglutaminase reaction by using a fluorescent amine, monodansyl cadaverine, as donor substrate and following the increase inExpand
αs1-Casein Film Prepared Using Transglutaminase
Transglutaminase is a Ca2 +-dependent enzyme that covalently polymerizes proteins through the formation of e-(γ-glutamyl)lysyl cross-links. We have reported that highly concentrated protein solutionsExpand
...
1
2
3
4
5
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