Purification and characterization of a novel thermostable 4-alpha-glucanotransferase of Thermotoga maritima cloned in Escherichia coli.

@article{Liebl1992PurificationAC,
  title={Purification and characterization of a novel thermostable 4-alpha-glucanotransferase of Thermotoga maritima cloned in Escherichia coli.},
  author={Wolfgang Liebl and Regina Feil and Josef Gabelsberger and Josef Kellermann and Karl Heinz Schleifer},
  journal={European journal of biochemistry},
  year={1992},
  volume={207 1},
  pages={81-8}
}
Maltodextrin glycosyltransferase (4-alpha-glucanotransferase) of the extremely thermophilic ancestral bacterium Thermotoga maritima has been purified from an Escherichia coli clone expressing the corresponding T. maritima MSB8 chromosomal gene. T. maritima 4-alpha-glucanotransferase, an approximately 53-kDa monomeric enzyme, is the most thermophilic glycosyltransferase described to date. It retained more than 90% of its maximum activity at temperatures from 55 degrees C up to 80 degrees C. The… CONTINUE READING