赤小豆芽超氧化物歧化酶的性质研究  

PURIFICATION AND CHARACTERIZATION OF SUPEROXIDE DISMUTASE IN SMALL RED BEAN

作　　者：檀志芬[1] 毛跟年[1] 葛超[1] 

机构地区：[1]陕西科技大学生命科学与工程学院,陕西咸阳712081

出　　处：《陕西科技大学学报（自然科学版）》2003年第2期27-29,共3页Journal of Shaanxi University of Science & Technology

摘　　要：采用硫酸铵分步沉淀 ,以 40 %硫酸铵饱和度去除杂蛋白 ,以 95 %硫酸铵饱和度沉淀酶蛋白。酶的耐热性一般 ,抗胰蛋白酶水解能力强 ,该酶在紫外光区的吸收峰为 2 75nm ,呈现Cu .ZnA superoxide dismutase from small red bean has been purified to homogeneity by ammonium sulfate fractionation . The results showed that 40% saturation degree was the best to remove impurity protein and 95% saturation degree was the best to deposit the enzyme protein.The enzyme has a weak sistance to temperature,and showed high n of Cu.Zn stability after degradation by trypsin . The iltravilet absorption spectral peak point of the enzyme is 275nm and appears the characteristic absorptio-SOD.

关 键 词：硫酸铵分步沉淀 赤小豆芽 超氧化物歧化酶 酶性质 

分 类 号：TS201.3[轻工技术与工程—食品科学]