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• W2361688778 abstract "A novel alkaline lipase was purified from a marine microorganism and the major physical and chemical characteristics of this alkaline lipase were studied and reported in this paper. Cell-free supernatant was prepared by centrifugation (4000r/min, 60min) of culture broth. After excess olive oil was extracted from the supernatant by the chloroform, the whole solution was centrifuged and some denatured proteins were removed from the supernatant. The supernatant was ultrafiltered using hollow fibers (100kD), the ultrafiltrate was then concentrated by ultrafiltration using a hollow fiber cartridge of 10kD cut off. The condensed lipase was purified 16.3-fold by means of CM Sepharose FF cationic-exchange chromatography by an elution with a linear gradient of 10mmol/L phosphate buffer (pH 3.8) containing 0.5mol/L NaCl. The purity of the purified lipase was confirmed by the presence of a single band on SDS-PAGE. The relative molecular mass of this enzyme was determined to be (38 0±1) kD. By the titrimetric method using olive oil as the substrate, characterization of the alkaline lipase was made. The lipase showed maximum activity at pH 8.5 and 35℃. When the temperature of the reaction system rose, there was a rapid decline of lipase activity; however, lipolytic activity dropped slowly with declining temperatures. 20% of lipase activity still remained at pH 8.5 and 5℃. According to the data mentioned above, lipase showed cold adapted and basophilic properties. In order to determine the K m and V max of the lipase, the lipolytic reaction was carried out using p-NPL as the substrate. The K m and V max of lipase under pH 8.5 and 35℃ were 7.805μmol/L and 1.2385mmol/(L·min), respectively. The enzyme was stable between pH 4.0 and 9.0 and at temperatures up to 35℃. In further studies, lipase showed good resistance to high salinities, the concentration of metal ions was up to 100mmol/L. Furthermore, lipase was compatible to some chemical regents. The lipase was stable in most polyhydroxy-compounds, in line with previous reports on lipases. Good resistance to the oxidant was also observed. Tween-40 could inhibit lipase activity significantly, while surfactant SDS could activate it. 10mmol/L EDTA could inhibit lipase activity seriously, it was speculated that there would be some metal ions in the active site of the lipase. When EDTA was added to the lipase standard assay system, metal ion amount was restrained or EDTA may cover the active site, thus, inactivate the lipase. In the further studies, the effect of Zn 2+ and EDTA on lipase activity was studied. The data indicated that some essential amino acid residue, which plays a key role in the catalytic mechanism, might bind with Zn 2+, resulting in lipase inactivation until Zn 2+ was chelated by EDTA." @default.
• W2361688778 created "2016-06-24" @default.
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• W2361688778 date "2004-01-01" @default.
• W2361688778 modified "2023-09-25" @default.
• W2361688778 title "PURIFICATION AND CHARACTERIZATION OF A LOW-TEMPERATURE ALKALINE LIPASE FROM MARINE MICROORGANISMS" @default.
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