Abstract.
A branching enzyme (EC 2.4.1.18) gene was isolated from an extremely thermophilic bacterium, Rhodothermus obamensis. The predicted protein encodes a polypeptide of 621 amino acids with a predicted molecular mass of 72 kDa. The deduced amino acid sequence shares 42–50% similarity to known bacterial branching enzyme sequences. Similar to the Bacillus branching enzymes, the predicted protein has a shorter N-terminal amino acid extension than that of the Escherichia coli branching enzyme. The deduced amino acid sequence does not appear to contain a signal sequence, suggesting that it is an intracellular enzyme. The R. obamensis branching enzyme was successfully expressed both in E. coli and a filamentous fungus, Aspergillus oryzae. The enzyme showed optimum catalytic activity at pH 6.0–6.5 and 65 °C. The enzyme was stable after 30 min at 80 °C and retained 50% of activity at 80 °C after 16 h. Branching activity of the enzyme was higher toward amylose than toward amylopectin. This is the first thermostable branching enzyme isolated from an extreme thermophile.
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Received revision: 5 September 2001
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Shinohara, M.L., Ihara, M., Abo, M. et al. A novel thermostable branching enzyme from an extremely thermophilic bacterial species, Rhodothermus obamensis . Appl Microbiol Biotechnol 57, 653–659 (2001). https://doi.org/10.1007/s00253-001-0841-3
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DOI: https://doi.org/10.1007/s00253-001-0841-3