韭菜过氧化物酶的分离纯化及性质  

Isolation, Purification and Characterization of Peroxidase from Chinese Chives

作　　者：敬海明[1] 邓玉[1] 成丽丽[1] 赵芯[1] 刘玉杰[1] 唐云明[1] 

机构地区：[1]西南大学生命科学学院,重庆市甘薯工程研究中心,三峡库区生态环境教育部重点实验室,重庆400715

出　　处：《食品科学》2012年第15期226-230,共5页Food Science

基　　金：重庆市科委重点攻关项目(CSTC2011AB1027)

摘　　要：经匀浆、抽提、硫酸铵分级沉淀、CM-Sepharose离子交换层析、Superdex-200凝胶过滤层析,获得电泳纯的韭菜过氧化物酶(POD)。该酶比活力达到14031.41U/mg,纯化倍数为102.96,回收率为10.85%。该酶分子质量约为28.4kD,最适温度40℃、最适pH值为4.6。该酶在20～40℃以及pH 4.0～8.0有较好的稳定性,在最适条件下测得其Km值为18.15mmol/L。低浓度草酸、Zn2+、Mg2+等对该酶有较强激活作用;甲醇、乙醇、异丙醇、SDS、抗坏血酸(AsA)以及Mn2+、Fe3+等对该酶有较强的抑制作用。Electrophoresis-pure peroxidase（POD） from Chinese chives was obtained after sample homogenization,extraction,ammonium sulfate precipitation,CM-Sepharose chromatography and Superdex-200 gel filtration.The purified POD had an activity of 14031.41U/mg.The purification factor was 102.96 and the recovery rate was 10.85%.The molecular weight of this enzyme was 28.4 kD,the optimum temperature and pH were 40 ℃ and 4.6,respectively.The POD enzyme was stable under 20-40℃ and pH 4-8.The Kmof this enzyme was determined to be 18.15 mmol/L under optimum conditions.Its activity could be strongly activated by low concentrations of oxalic acid,Zn2＋and Mg2＋,but inhibited by methanol,ethanol,isopropanol,SDS,ascorbic acid,Mn2＋and Fe3＋.

关 键 词：韭菜 过氧化物酶 分离纯化 性质 

分 类 号：Q554.6[生物学—生物化学]