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花生几丁质酶的纯化及酶学性质研究
引用本文:李奕雅,;陈凡,;汪少芸,;叶秀云,;陈躬瑞,;饶平凡. 花生几丁质酶的纯化及酶学性质研究[J]. 漳州师院学报, 2008, 0(3): 79-83
作者姓名:李奕雅,  陈凡,  汪少芸,  叶秀云,  陈躬瑞,  饶平凡
作者单位:[1]漳州师范学院生物科学与技术系,福建漳州363000; [2]福州大学生物科学与工程学院,福建福州350002
基金项目:福建省教育厅资助项目(JB05040)
摘    要:本课题利用亲和色谱和凝胶过滤色谱法从花生种子中分离得到了几丁质酶.经SDS-PAGE鉴定,该酶蛋白已达电泳纯,分子量约34.4 kD.在还原和非还原状态下均显示单一区带,表明其为单体蛋白.此外,通过等电聚焦法可测得该酶等电点为5.1.而酶学性质的相关研究则表明:该酶最适pH为5.4,最适反应温度为40~50℃.

关 键 词:花生  几丁质酶  纯化  表征

Purification and Enzymatic Characterization of the Chitinase from Arachis hpyogaea
Affiliation:LI Yi-ya , CHEN Fan , WANG Shao-yun, YE Xiu-yun , CHEN Gong-rui , RAO Ping-fan (1.Department of Biology Science and Technology, Zhangzhou Normal University, Zhangzhou, Fujian 363000, China; 2.College of Biological Science and Technology, Fuzhou University, Fuzhou, Fujian 350002, China)
Abstract:A chitinase was purified from seeds of peanut (Arachis hpyogaea) by aqueous extraction, affinity chromatography (Affi-gel) and Gel-filtration chromatography (Sephadex G-75). The purified enzyme showed a single band on SDS-PAGE with the molecular weight about 34.4 kD in both reduced and non-reduced conditions, indicating that the enzyme is a monomeric protein. The pI was measured to be 5.1 by isoelectric focusing electrophoresis. The enzyme exhibited its optimum activity at pH 5.4, and a temperature between 40℃ and 50℃.
Keywords:peanut  chitinase  purification  characterizartion
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