Journal
BIOTECHNOLOGY LETTERS
Volume 36, Issue 6, Pages 1295-1302Publisher
SPRINGER
DOI: 10.1007/s10529-014-1475-8
Keywords
Arctic bacterium; Bacillus pumilus; Lipase; Psychrophilic lipase; Rational mutation
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Funding
- Ministry of Oceans and Fisheries [PM12030]
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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 A degrees C, respectively. The enzyme retained 85 % of its activity at 5 A degrees C. There was a significant difference between temperatures for maximal activity (20 A degrees C) and for protein denaturation (approx. 45 A degrees 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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