Format

Send to

Choose Destination
See comment in PubMed Commons below
Appl Microbiol Biotechnol. 2004 May;64(4):447-54. Epub 2004 Jan 22.

Properties and applications of microbial transglutaminase.

Author information

1
Ajinomoto Institute of Life Sciences, 1-1 Suzuki-cho, Kawasaki-ku, 210-8681 Kawasaki, Japan.

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.

PMID:
14740191
DOI:
10.1007/s00253-003-1539-5
[Indexed for MEDLINE]
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Springer
    Loading ...
    Support Center