食品工业科技Issue(1)：95-99,5.
鸭肝丁酰胆碱酯酶的纯化与酶学性质研究
Purification and Characterization of the butyrylcholinesterase from duck liver
摘要
Abstract
Objective:To obtain butyrylcholinesterase from duck liver and study on the characterization of the purified product. Methods: The butyrylcholinesterase was extracted by acetone treatment, acid precipitation, ammonium sulfate precipitation, and ion-exchange chromatography on DEAE-Sepharose and gel filtration on Sephacryl S-200. SDS-PAGE was used to identify the purity and relative molecular of the butyrylcholinesterase. Results : The enzyme was purified to electrophoretic homogeneity. It was purified 156.45-fold and the activity recovery 23.60％ was obtained. Its specific activity was 17.21 U/mg. The relative molecular weight of this butyrylcholinesterase was 388.85kDa,and the weight of subunit was 64.70kDa. The butyrylcholinesterase consisted of six identical subunits.Ultraviolet spectrum showed a maximum absorption at 278nm. The optimum pH and temperature of the enzyme for the hydrolysis of S- Butyrylthiocholine iodide were 8.0 and 35℃, respectively. The enzyme was stable in the pH ranges of 3.0～10.0 under 35℃ and at temperatures below 45℃. Zn2+ , Mn2+ ,Cu2+ had significant inhibition on this enzyme and the enzyme could not be inhibited by excess substrate. The apparent Km of this enzyme was 71.15μmol/L at pH8.0 and 35℃. Conclusion: The butyrylcholinesterase was successfully purified, and this butyrylcholinesterase showed good acid-base tolerance.关键词
鸭肝/丁酰胆碱酯酶/分离纯化/性质分类
轻工纺织引用本文复制引用
朱鸿,李想韵,邓玉,王松,付伟丽,唐靓婷,诰赵伟,唐云明..鸭肝丁酰胆碱酯酶的纯化与酶学性质研究[J].食品工业科技,2011,(1):95-99,5.基金项目
重庆市科委资助项目(CSCT,2004AC1012). （CSCT,2004AC1012）
