Purification and Characterization of a Novel Lipase from Antarctic Krill |
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| Authors: | CHEN Xin WANG Chunlan XU Jiakun WANG Fang JIANG Yihui CHEN Yixuan and ZHAO Xianyong |
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| Institution: | College of Food Science and Technology,Shanghai Ocean University,Shanghai 201306,China;Yellow Sea Fisheries Research Institute,Chinese Academy of Fishery Sciences,Key Laboratory of Sustainable Development of Polar Fishery,Ministry of Agriculture and Rural Affairs of PRC,Qingdao 266071,China;Yellow Sea Fisheries Research Institute,Chinese Academy of Fishery Sciences,Key Laboratory of Sustainable Development of Polar Fishery,Ministry of Agriculture and Rural Affairs of PRC,Qingdao 266071,China;Yellow Sea Fisheries Research Institute,Chinese Academy of Fishery Sciences,Key Laboratory of Sustainable Development of Polar Fishery,Ministry of Agriculture and Rural Affairs of PRC,Qingdao 266071,China;Laboratory for Marine Drugs and Bioproducts of Qingdao National Laboratory for Marine Science and Technology,Qingdao 266237,China;Yellow Sea Fisheries Research Institute,Chinese Academy of Fishery Sciences,Key Laboratory of Sustainable Development of Polar Fishery,Ministry of Agriculture and Rural Affairs of PRC,Qingdao 266071,China;College of Chemistry and Chemical Engineering,Ocean University of China,Qingdao 266100,China;Yellow Sea Fisheries Research Institute,Chinese Academy of Fishery Sciences,Key Laboratory of Sustainable Development of Polar Fishery,Ministry of Agriculture and Rural Affairs of PRC,Qingdao 266071,China;Laboratory for Marine Fisheries Science and Food Production Processes,Qingdao National Laboratory for Marine Science and Technology,Qingdao 266071,China |
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| Abstract: | Lipase from Antarctic krill, with a molecular weight of 71.27 kDa, was purified with ammonium sulfate precipitation and a series of chromatographic separations over ion exchange（DEAE） and gel filtration columns（Sephacryl S-100）, resulting in 5.2% recovery with a 22.4-fold purification ratio. The optimal pH and temperature for enzyme activity were 8.0 and 45℃, respectively. Purified lipase had Km and Vmax values of 3.27 mmol L-1 and 2.4 U mg-1, respectively, using p-nitrophenyl laurate as the substrate. Lipase activity was enhanced by adding Ca2+ and Mg2+ ions in the concentration ranges of 0–0.5 mmol L-1 and 0–0.3 mmol L-1, respectively, while the activity was inhibited by a further increase in these ion concentrations. Fe3+ and Cu2+ ions showed obvious inhibitory effects on enzyme activity, and the inhibition rates were 71.8% and 53.3% when the ion concentrations were 0.5 mmol L-1. |
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| Keywords: | Antarctic krill lipase isolation and purification enzymology properties |
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