Characterization and a point mutational approach of a psychrophilic lipase from an arctic bacterium, Bacillus pumilus
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- Characterization and a point mutational approach of a psychrophilic lipase from an arctic bacterium, Bacillus pumilus
- Wi, Ah Ram
Park, Ha Ju
Han, Se Jong
Yim, Joung Han
- Biotechnology & Applied Microbiology
- Arctic bacterium; Bacillus pumilus; Lipase; Psychrophilic lipase; Rational mutation
- Issue Date
- Wi, Ah Ram., et al. 2014. Characterization and a point mutational approach of a psychrophilic lipase from an arctic bacterium, Bacillus pumilus. Biotechnology Letters, 36(6): 1295-1302.
- A bacterium with lipolytic activity was isolated from the Chukchi Sea within the Arctic Ocean. The lipase BpL5 from the isolate, Bacillus pumilus ArcL5, belongs to subfamily 4 of lipase family I. The optimum pH and temperature of the
recombinant enzyme BpL5, as expressed in Escherichia coli, were 9.0 and 20℃, respectively. The enzyme retained 85 % of its activity at 5 ℃. There was a significant difference between temperatures for maximal activity (20℃) and for protein denaturation (approx. 45℃). The enzyme preferred middle-chain
(C8) p-nitrophenyl substrates. Two mutants, S139A
and S139Y, were rationally designed based on the 3D structure
model, and their activities were compared
with that of the wild type. The both mutants showed
significantly improved activity against tricaprylin.
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