Title: Purification and Enzymatic Characters of Low-temperature Lipase from Bacillus phychrophilus
Abstract: This study involves purification of a wild low-temperature lipase from a strain of Bacillus phychrophilus and analysis of its enzymatic characters.Electrophoretic pure enzyme on the SDS-PAGE was obtained through ammonium sulfate precipitation,phenyl superpose hydrophobic chromatography and Q FF anion-exchange chromatography.The optimum temperature of the enzyme is 25℃,which still has 25% relative lipase activity at 0℃.The activity of the lipase almost completely lost after incubation at 60℃ for 30 min.Lipase activity is independent of divalent cation.And the structure of this lipase may contain disulfide bond.The K-m and V-max of lipase under pH8.0 and 25℃ were 2.65×10-5mol/L and 5.21mmol/(L·min)respectively.
Publication Year: 2007
Publication Date: 2007-01-01
Language: en
Type: article
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