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Position: Home > Articles > Isolation, Purification and Characterization of Peroxidase from Cucumber FOOD SCIENCE 2014,35 (11) 168-173

黄瓜过氧化物酶的分离纯化及酶学性质

作  者：
胡瑞斌;李星;王红杨;王洁;唐云明
单  位：
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
关键词：
黄瓜;过氧化物酶;分离纯化;性质
摘  要：
新鲜的黄瓜经匀浆、抽提、硫酸铵沉淀、CM-Sepharose离子交换层析、Superdex-200凝胶过滤层析后获得电泳纯的过氧化物酶。该酶的比活力、回收率及纯化倍数分别为64 177.67 U/mg、9.58%、61.93。该酶的分子质量为41.15 kD,亚基分子质量为40.21 kD。该酶的最适温度和最适pH值分别为60℃和6。在25~45℃及pH 5~9的范围内非常的稳定。在测定条件下测得该酶的Km值为53.79 mmol/L。硫氰化钾对该酶活力基本无影响。尿素、K+、Mn2+、Ca2+、Mg2+、Ba2+、Cu2+对该酶都具有激活作用且浓度至50 mmol/L时酶活力分别被激活至112%、127%、113%、128%、139%、199%、348%,然而十二烷基磺酸钠、抗坏血酸和草酸对该酶有强烈的抑制作用;Zn2+、甲醇、乙醇和异丙醇对该酶有一定的抑制作用。
译  名：
Isolation, Purification and Characterization of Peroxidase from Cucumber
作  者：
HU Rui-bin;LI Xing;WANG Hong-yang;WANG Jie;TANG Yun-ming;Key Laboratory of Eco-environments in Three Gorges Reservoir Region, Ministry of Education, Chongqing Sweet-Potato Engineering Research Center, School of Life Sciences, Southwest University;
关键词：
cucumber;;peroxidase;;isolation and purification;;characterization
摘  要：
Electrophoresis-purity peroxidase was extracted from fresh cucumber and purified through homogenization, extraction, ammonium sulfate precipitation, CM-Sepharose and Superdex-200 chromatography. The specific activity, recovery and purification fold of the peroxidase were 64 177.67 U/mg, 9.58% and 61.93, respectively. Molecular mass of this purified enzyme was 40.21 kD as determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis(SDS-PAGE), while native gel filtration confirmed a monomer form of 41.15 kD. Besides, the peroxidase, whose optimum temperature and pH were 60 ℃ and 6, respectively, was comparatively stable in the temperature range of 25-45 ℃ and pH range of 5-9. The purified peroxidase showed Km value of 53.79 mmol/L under definite conditions. In addition, its activity was scarcely affected by potassium thiocyanate(KSCN). The peroxidase was found to be activated by urea, K+, Mn2+, Ca2+, Mg2+, Ba2+and Cu2+ by 12%, 27%, 13%, 28%, 39%, 99% and 248% at 50 mmol/L, respectively. However, the peroxidase activity was significantly inhibited by SDS, ascorbic acid and oxalic acid. Moreover, Zn2+, methanol, ethanol and isopropanol caused partial inhibitory effects on the peroxidase.

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