漆树漆酶两种同工酶分离纯化与特性研究

漆树漆酶两种同工酶分离纯化与特性研究 Study on Purification and Characterization of Two Isoforms ofChinese Rhus Laccases from Rhus vernicifera 万云洋 WAN Yun-yang 1 1 2 3 first-author 杜予民 DU Yu-min 1 1 2 3 杨建红 YANG Jian-hong 1 1 2 3 陈荣智 CHEN Rong-zhi 2 1 2 3 肖玲 XIAO Ling 1 1 2 3 张艳 ZHANG Yan 2 1 2 3 武汉大学资源与环境科学学院 武汉大学资源与环境科学学院 College of Resources and Environmental Sciences, Wuhan University College of Resources and Environmental Sciences, Wuhan University 武汉大学生命科学学院 武汉大学生命科学学院 College of Life Sciences, Wuhan University College of Life Sciences, Wuhan University 武汉大学生命科学学院,湖北,武汉,430072 武汉大学生命科学学院,湖北,武汉,430072 应用柱层析和HPLC方法从漆树漆液中分离提纯漆酶的两种同工酶L1和L2 .两者均为低温酶 ,最适的温度分别为 2 0℃和 13℃ ,pH值分别为 6.7和 7.2 ,等电点分别为 8.6和 9.1.通过十二烷基硫酸钠 聚丙烯酰胺凝胶电泳 ,测得它们的分子量分别为 1.2× 10 5和 1.0 5× 10 5.两种酶均不能催化氧化间氨基苯甲酸 ,对 3 氨基酪氨酸等有很高的反应活性 Two isoforms of laccase were obtained as the main phenol-oxidases from latex of Chinese lacquer tree Rhus vernicifera. Both of L1 and L2 were low-temperature enzymes with optimum temperature 20℃ and 13℃ respectively. The laccases had very narrow optimal pH, and more stable at neutral pH than at basic pH, each with pI 8.6 and 9.1. The molecular masses of the purified laccases were about 1.2×10 5 and 1.05×10 5 by sodium dodecyl sulfate polyacrylamide gel electrophoresis （SDS-PAGE）. Both of L1 and L2 can catalyze 3-amino tyrosine, but not to m-amniobenzoic acid. 漆树漆酶 同工酶 特性 Rhus laccase isoforms properties Q554.9 国家自然科学基金资助项目 （ 30 170 75 7） 2003-02-01 2021-04-01 2