部分观赏植物苯丙氨酸解氨酶的初步研究  

A primary study on phenylalanine ammonia lyase in some ornamental plants

作　　者：曹锦萍[1] 吕培涛[1] 程桂平[1] 刘季平[1,2] 贺立红[1] 何生根[1] 

机构地区：[1]仲恺农业工程学院生命科学院,广东广州510225 [2]华南农业大学园艺学院,广东广州510642

出　　处：《仲恺农业工程学院学报》2009年第4期14-18,共5页Journal of Zhongkai University of Agriculture and Engineering

基　　金：国家自然科学基金(30771519);教育部留学回国人员启动基金(2007-1108);广东省自然科学基金(8251022501000002);广州市重点科技攻关(2007Z2-E0071);广州市荔湾区科技计划(2008210021)资助项目

摘　　要：检测了几种观赏植物的苯丙氨酸解氨酶（Phenylalanine ammonia lyase,PAL）活性的分布,并采用硫酸铵沉淀法着重对茉莉[Jasminum sambac（L.）Aiton]叶片中的PAL进行分离提纯及对部分酶学性质进行研究.结果表明,该酶在所检测的植物不同器官中均有分布.其中,茉莉叶片中的PAL活性最高;50%饱和度的硫酸铵一步沉淀能使91%的酶蛋白沉淀下来,20%-60%饱和度的硫酸铵分级沉淀能使初酶液纯化31.1倍;茉莉PAL催化其底物L-苯丙氨酸（L-Phe）裂解反应的最适pH为8.8、最适温度为35℃;PAL酶活性与底物Phe浓度的关系符合米氏动力学.The distribution of phenylalanine ammonia lyase（PAL,EC4.3.1.5）activity in some ornamental plants was detected and the partial purification with ammonia sulfate precipitation and characterization of the PAL from jasmine（Jasminum sambac（L.）Aiton）leaves were investigated.The results showed that PAL widely existed in different organs of tested plants.Additionally,it was found that the PAL activity was especially high in jasmine leaves.One-step precipitating with 50% ammonium sulphate could obtain 91.9% of PAL activity and the purification factor was 3.8-fold;Two-step precipitating with 20%~60% ammonium sulphate fractionation could obtain 39.5% of PAL activity and the purification factor reached to 31.1-fold.Optimum reaction temperature and pH for PAL was 35 ℃ and 8.8,respectively.The function between the PAL activity and its substrate L-phenylalanine concentration agreed with Michaelis-Menten kinetics.

关 键 词：苯丙氨酸解氨酶 茉莉(Jasminum sambac) 酶活性 

分 类 号：Q945[生物学—植物学]