淡江大學機構典藏:Item 987654321/51817
English  |  正體中文  |  简体中文  |  全文笔数/总笔数 : 62830/95882 (66%)
造访人次 : 4037771      在线人数 : 551
RC Version 7.0 © Powered By DSPACE, MIT. Enhanced by NTU Library & TKU Library IR team.
搜寻范围 查询小技巧:
  • 您可在西文检索词汇前后加上"双引号",以获取较精准的检索结果
  • 若欲以作者姓名搜寻,建议至进阶搜寻限定作者字段,可获得较完整数据
  • 进阶搜寻


    jsp.display-item.identifier=請使用永久網址來引用或連結此文件: https://tkuir.lib.tku.edu.tw/dspace/handle/987654321/51817


    题名: 含澱粉酶菌(Exiguobacterium sp.)的分離、鑑定與特性分析
    其它题名: Isolation and characterization of α-amylase containing bacteria (Exiguobacterium sp.)
    作者: 宋君陵;Sung, Chun-ling
    贡献者: 淡江大學生命科學研究所碩士班
    簡素芳;Chien, Su-fang
    关键词: 澱粉酶;Exiguobacterium sp;α-Amylase;Exiguobacterium sp
    日期: 2010
    上传时间: 2010-09-23 16:10:28 (UTC+8)
    摘要: α-澱粉酶家族擁有三項共同特徵:在α-糖甘鍵上作用、擁有包含催化端的花籃狀蛋白結構、基因上有4個高度保留區分別和形成催化端與穩定花籃狀蛋白構形有關。本實驗利用基因轉殖方法,嘗試轉殖α-澱粉酶基因片段,透過隨機水解細菌染色體、轉殖入宿主細胞,製做Exiguobacterium sp.的基因圖譜,並以活性染色方式篩選菌株。成功轉殖的片段再經過修飾後轉殖入表達載體,配和表達宿主經過1 mM IPTG誘導後,透過蛋白質膠體染色可看出酵素明顯活性增加。
    原菌酵素活性測試為48.82 U/mg,酵素最適pH為6,最適反應溫度為37℃。
    The α-amylase family has three common features:Act on α-glycosidic bonds and hydrolyze the bond to α-anomeric oligosacchrides or forming α-1,4 or α-1,6 bond、they all have the (β/α)8 or TIM barrel protein structure
    contain the catalytic site、all of them have four highly conserved regions in their primary sequence which contain the amino acids that form the catalytic site and TIM barrel.
    DNA library was made by using partial digestion to digest Exiguobacterium sp. chromosome.Then clone into host cell selected by activity staining. Modified the sequence and clone again into pET expression vector system. Add 1 mM IPTG for induce a large amount of protein. Primary supernatant of Exiguobacterium sp. was concentrate and test by DNSA. The special activity was 48.82 U/mg. While the condense supernatant has the optimal condition on pH 6 and 37℃.
    显示于类别:[生命科學研究所] 學位論文

    文件中的档案:

    档案 大小格式浏览次数
    index.html0KbHTML434检视/开启

    在機構典藏中所有的数据项都受到原著作权保护.

    TAIR相关文章

    DSpace Software Copyright © 2002-2004  MIT &  Hewlett-Packard  /   Enhanced by   NTU Library & TKU Library IR teams. Copyright ©   - 回馈