A highly thermostable endo-(1,4)-β-mannanase from the marine bacterium Rhodothermus marinus

  title={A highly thermostable endo-(1,4)-β-mannanase from the marine bacterium Rhodothermus marinus},
  author={O. Politz and Martin Krah and Karl Kristian Thomsen and Rainer Borriss},
  journal={Applied Microbiology and Biotechnology},
Rhodothermus marinus ATCC 43812, a thermophilic bacterium isolated from marine hot springs, possesses hydrolytic activities for depolymerising substrates such as carob-galactomannan. Screening of expression libraries identified mannanase-positive clones. Subsequently, the corresponding DNA sequences were determined, eventually identifying a coding sequence specifying a 997 amino acid residue protein of 113 kDa. Analyses revealed an N-terminal domain of unknown function and a C-terminal… CONTINUE READING
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