节点文献

非水介质中多酚氧化酶催化羟基化反应的研究

Study on Hydroxylation Reaction Catalyzed by Polyphenoloxidase in Nonaqueous Media

  • 推荐 CAJ下载
  • PDF下载
  • 不支持迅雷等下载工具,请取消加速工具后下载。

【作者】 由德林曹淑桂马林

【Author】 YOU De\|lin\+1, CAO Shu\|gui\+1, MA Lin\+2 (1. Laboratory of Enzyme Engineering, Jilin University, Changchun 130021, China; 2. Department of Applied Chemistry, Zhongshan University, Guangzhou 510275, China)

【机构】 吉林大学酶工程实验室!吉林长春130021中山大学应用化学系!广东广州510275

【摘要】 以对甲酚为底物 ,利用从马铃薯中提取的多酚氧化酶的粗酶液 ,用多孔玻璃包衣琼脂疏水吸附法将多酚氧化酶固定化 ,并利用此固定化酶 ,考察了在非水介质中羟基化反应的最适宜条件 .在此条件下催化合成 4-甲基邻苯二酚的产率为 5 5 .8%

【Abstract】 Besides in nonaqueous enzymology, polyphenoloxidase can also be used in analytical chemistry as the enzyme electrode to identify phenols and cyanide, etc. The polyphenoloxidase inhibitors are widely used in industries of cosmotics and food. Polyphenoloxidase can change L \|tyrosin into L \|DoPA, a routine medicine for Pakinson’s disease. Tyrosonase has the character of ortho\|hydroxylation on benzene ring, so it has great significance in organic synthesis. Owing to its importance in medicine, the catalytic conversions of p \|cresol to 4\|methyl catechol and catechols to 4\|methyl\|1,2\|benzoquinone were intensively studied. In this work, we used a chemical method to reduce 4\|methyl\|1,2\|benzoquinone to 4\|methyl catechol, and to optimize the reaction conditions of catechol synthesis catalyzed by immobilized enzyme. The yield of 4\| methyl catechol catalyzed by immobilized enzyme is 55.8%.

  • 【文献出处】 分子催化 ,Journal of Molecular Catalysis (China) , 编辑部邮箱 ,2001年03期
  • 【分类号】O621
  • 【被引频次】3
  • 【下载频次】134
节点文献中: