一种麦芽酸性磷酸酶的分离纯化及部分性质研究  

Purification and some properties of wheat germ acid phosphatase

作　　者：杨彩兰[1] 陈巍[1] 苟春宝[1] 王勇[1] 魏炜[1] 

机构地区：[1]四川大学生命科学学院生物资源与生态环境教育部重点实验室,成都610065

出　　处：《四川大学学报（自然科学版）》2011年第1期206-212,共7页Journal of Sichuan University(Natural Science Edition)

基　　金："十一五"国家科技支撑计划重点项目(2006BAF07B01)

摘　　要：经硫酸铵分级沉淀、CM-Sepharose CL 4B和DEAE-Sepharose CL 4B离子交换柱层析等步骤,从麦芽中分离提纯到一种酸性磷酸酶(ACPase,E.C.3.1.3.2),纯化倍数为33.06,酶液比活为88.27 U/mg.通过动力学方法测得其最适pH为5.4,酸碱稳定性较差,仅在pH6.0左右的缓冲液中较稳定;最适温度为50℃,40℃以下有较好的稳定性;在最适条件下,该酶催化pNPP的米氏常数(K_m)为4.696×10^(-4)mol/L.同时研究了一些金属离子和有机化合物对该酶活性的影响.A kind of acid phosphatase was purified from wheat germ. Some properties of the enzyme had been studied. The enzyme was obtained by ammunium sulfate fractionation, CM-Sepharose CL 4B ion- exchange chromatography and DEAE-Sepharose CL 4B ion-exchange chromatography. The purification multiple was 33.06 and the specific activity was 88.27 U/mg. The optimum pH and optimum tempera- ture were pH 5.4 and 50 ℃ respectively. Stability range of pH was just about 6.0. The enzyme was sta- ble below 40 ℃. The Km of pNPP as substrate was 4. 696×10^-4mol/L at pH 5.4 and 50 ℃. The effects of some metal ions and organic compounds on the enzyme activity were studied.words,

关 键 词：麦芽 酸性磷酸酶 分离纯化 动力学性质 

分 类 号：Q555[生物学—生物化学]