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Purification and biochemical characterization of a cold-active lipase from Antarctic sea ice bacteria Pseudoalteromonas sp. NJ 70
- Wang, Quanfu, Hou, Yanhua, Ding, Yu, Yan, Peisheng
- Molecular biology reports 2012 v.39 no.9 pp. 9233-9238
- Pseudoalteromonas, bacteria, barium, calcium, copper, detergents, esters, ice, iron, lead, magnesium, manganese, molecular weight, octoxynol, pH, polyacrylamide gel electrophoresis, polysorbates, sodium chloride, temperature, thiourea, triacylglycerol lipase, zinc, Antarctic region
- 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.