莲藕过氧化物酶的分离纯化及性质研究  

Isolation,Purification and Properties of Peroxidase from Lotus (Nelumbo nucifera Gaertn.) Root

作　　者：阙瑞琦[1] 张丽丽[1] 郭小路[1] 唐云明[1] 

机构地区：[1]西南大学生命科学院,重庆400715

出　　处：《西南大学学报（自然科学版）》2007年第12期63-67,共5页Journal of Southwest University(Natural Science Edition)

基　　金：重庆市科委资助项目(CSTC;2004AC1012).

摘　　要：经40%-85%硫酸铵分级沉淀、DEAE-Sepharose离子交换层析、Sephacryl S-200凝胶过滤层析纯化,得到莲藕过氧化物酶（POD）电泳纯制品.该酶纯化倍数为39.77倍,回收率为11.76%.酶学性质和动力学性质研究表明,该酶最适pH为5.0;最适温度为35℃;以不同浓度的过氧化氢与莲藕POD在25℃、pH5的条件下反应,测得其Km值为9mmol/L.CuSO4和ZnSO4对莲藕POD活性有激活作用;BaCl2、MgCl2及SDS对其活性影响不大;Na2SO4、Li2SO4、KCl和NaCl对POD活性有一定的抑制作用;MnSO4和FeSO4对POD活性有较强的抑制作用;ASA能完全抑制POD的活性.Using ammonium sulfate precipitation, ion exchange chromatography on DEAE-Sepharose Fast Flow column and gel filtration chromatography on Sephacryl S-200, purified peroxidase （POD） from lotus （Nelumbo nucifera Gaertn. ） root was obtained, with a purification ratio of 39.77 and a recovery yieid of 11.9%. Kinetic study showed that the optimum pH and temperature for the enzyme was pH 5.0 and 35℃, respectively. The apparent Km values of the enzyme with different concentrations of H2O2 as the substrate was 9 mmol/L at 25 ℃ and pH 7.2. CuSO4 and ZnSO4 enhanced POD activity. BaCle, MgCle and SDS didn＇t affect POD activity obviously. Na2 SO4, Li2 SO4, KCl and NaCl partially inhibited POD activity. MnSO4 and FeSO4 inhibited POD activity seriously. Furthermore, ASA inhibited POD activity completely.

关 键 词：莲藕 过氧化物酶 分离纯化 性质 

分 类 号：S645.1[农业科学—蔬菜学]