食品科学 贻贝过氧化氢酶的纯化及部分性质.pdfVIP

22 2000,Vol.21,No.11 食品科学 基 础 研 究 贻贝过氧化氢酶的纯化及部分性质 林少琴 兰瑞芳 余萍 程蔚 福建师范大学实验中心 福州 350007 摘 要 新鲜贻贝肉匀浆抽提液经硫酸铵盐析 DEAE-Sepharose FF柱层析纯化 得到一种过氧化氢酶 该酶 为糖蛋白 亚基分子量约为76000 中性糖含量约为10.56% 研究结果表明 贻贝过氧化氢酶的最佳pH7.0左右 对热不稳定 45 保温15min 酶的残余活力约为70% 60 保温15min 则酶的残余活力仅剩10.6%左右 NaN 3 2+ 2+ 2+ 2+ 2+ 2+ 2+ KCN及某些金属离子如Pb Hg Fe Cd 等抑制酶的活性 Zn Cu Mg 则对酶有不同程度的激活作用 关 键 词 贻贝 过氧化氢酶 糖蛋白 纯化 性质 A b s t r a c t A catalase from fresh Perna Viridis had been purified by the use of saline extraction,ammonium sulfate precipition and DEAE-Sepharose FF column chromatography.It was identi- fied as glycoprotein and the neutral saccharide content of the enzyme was assayed as about 1056% .The enzyme subunit molecular weight was about 76000 as determined by SDS-polyacrylamide gel electrophoresis.The experiment result indicated that the optimal temperatme and pH of the enzyme were 35 and 7 respectively.The enzyme was not stable in heat and retained 70% of the original enzyme activity after incubation at 45 for 15min .It had only 10.6% of the original enzyme activity after incubation at 60 for 15min .Its catalytic activity was strongly inhibited by NaN 3 2+ 2+ 2+ 2+ 2+ 2+ 2+ 2+ and KCN The metal ions Pb Hg Fe Cd Ni showed some inhibition and Zn Cu Mg could increase its activity in varying degrees. K e y w o r d Perna Viridis Catalase Glyc