详细信息
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
文献类型:期刊文献
中文题名:十二节杆菌胞外脂肪酶的纯化和性质研究
英文题名:Production,purification and properties of an extracellular lipase from Arthrobacter duodecadis
作者:唐芸[1];宋庆训[1];李晓敦[1];沈亚领[1];魏东芝[1]
机构:[1]华东理工大学生物反应器工程国家重点实验室生物化学研究所,上海200237
年份:2007
卷号:37
期号:4
起止页码:45
中文期刊名:工业微生物
外文期刊名:Industrial Microbiology
收录:北大核心:【北大核心2004】;CSCD:【CSCD2011_2012】;
语种:中文
中文关键词:十二节杆菌;脂肪酶;疏水层析;纯化
外文关键词:Arthrobacter duodecadis; hydrophobic interaction chromatography; lipase;purification
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。
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^++.
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