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Updated: May 2, 2026

Defining Substrate Specificities for Lipase and Phospholipase Candidates
Published on: November 23, 2016
Characterization and a point mutational approach of a psychrophilic lipase from an arctic bacterium, Bacillus pumilus
Ah Ram Wi1, Sung-Jong Jeon, Sunghui Kim
1Division of Life Sciences, Korea Polar Research Institute (KOPRI), 26, Songdomirae-ro, Yeonsu-gu, Incheon, 406-840, Republic of Korea.
Abstract:
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 °C, respectively. The enzyme retained 85 % of its activity at 5 °C. There was a significant difference between temperatures for maximal activity (20 °C) and for protein denaturation (approx. 45 °C). 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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