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十二节杆菌胞外脂肪酶的纯化和性质研究
Production,purification and properties of an extracellular lipase from Arthrobacter duodecadis
【摘要】 十二节杆菌发酵得到的胞外脂肪酶,在5L发酵罐经过34h培养,最高酶活可达75 U/mL。通过硫酸铵梯度沉淀和疏水层析纯化,脂肪酶纯化26倍,总得率24.3%。SDS-PAGE显示脂肪酶分子量为33 kD,脂肪酶在40℃和pH 7.0时酶活力最高,同时在24℃经过48h仍保持一半左右的活力。该脂肪酶的酶活受K+,Mg2+激活,而受Zn2+与Co2+的抑制。
【Abstract】 After Arthrobacter duodecadis cultured at 28℃ for 34h,the extracellular lipase with enzyme activity of 75U/mL was obtained.The lipase was purified by ammonium sulfate fraction and hydrophobic interaction chromatography to result in a 26-fold purification with 24.3% of final yield.The molecular weight of the enzyme was determined to be 33 kD by SDS-PAGE.The enzyme exhibited maximum activity at 40℃ and pH 7.0 and kept above 50% activity over 48 h at 24℃.The enzyme activity was promoted in the presence of K+,Mg++ and was inhibited by Zn++,Co++.
【Key words】 Arthrobacter duodecadis; hydrophobic interaction chromatography; lipase; purification;
- 【文献出处】 工业微生物 ,Industrial Microbiology , 编辑部邮箱 ,2007年04期
- 【分类号】TQ925
- 【被引频次】7
- 【下载频次】249