, Volume 39, Issue 9, pp 9233-9238

Purification and biochemical characterization of a cold-active lipase from Antarctic sea ice bacteria Pseudoalteromonas sp. NJ 70

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Abstract

An extracellular cold-active lipase from Antarctic sea ice bacteria Pseudoalteromonas sp. NJ 70 was purified and characterized. The overall purification based on lipase activity was 27.5-fold with a yield of 25.4 %. The purified lipase showed as a single band on SDS-PAGE with an apparent molecular weight of 37 kDa. The optimum temperature and pH were 35 °C and 7.0, respectively. The lipase activity was enhanced by Ca2+ and Mg2+, while was partially inhibited by other metals such as Cu2+, Zn2+, Ba2+, Pb2+, Fe2+ and Mn2+. The lipase had high tolerance to a wide range of NaCl concentrations (0–2 M NaCl). It exhibited high levels of activity in the presence of DTT, Thiourea, H2O2 as well as in the presence of various detergents such as Span 60, Tween-80, Triton X-100. In addition, the lipase showed a preference for long-chain p-nitrophenyl esters (C12–C18). These results indicated that this lipase could be a novel cold-active lipase.