National Taiwan Ocean University Institutional Repository:Item 987654321/37730
English  |  正體中文  |  简体中文  |  全文笔数/总笔数 : 27228/39071
造访人次 : 2408804      在线人数 : 72
RC Version 4.0 © Powered By DSPACE, MIT. Enhanced by NTU Library IR team.
搜寻范围 进阶搜寻

jsp.display-item.identifier=請使用永久網址來引用或連結此文件: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/37730

题名: Taiwanofungus camphorata nitroreductase: cDNA cloning and biochemical characterisation
作者: Chih-Chen Chen;Chuian-Fu Ken;Lisa Wen;Ching-Fong Chang;Chi-Tsai Lin
贡献者: 國立台灣海洋大學:生命科學系
关键词: Taiwanofungus camphorata;Nitroreductase;Three-dimension structural model (3-D structural model)
日期: 2012-12
上传时间: 2016-05-02T06:41:21Z
出版者: Food Chemistry
摘要: Abstract:Nitroreductases (Nrs) play important roles in redox system via NADPH or NADH as a reductant. A TcNr cDNA encoding a putative Nr was cloned from Taiwanofungus camphorata. A 3-D structural model of the TcNr has been created based on the known structure of BcNr (Bacillus cereus). To characterise the TcNr, the coding region was subcloned into an expression vector and transformed into Escherichia coli. The recombinant His6-tagged TcNr was purified by Ni affinity chromatography. The purified enzyme showed a single band at molecular mass of approximately 25 kDa on 12% sodium dodecyl sulphate–polyacrylamide gel electrophoresis. The enzyme exhibited Nr activity via ferricyanide assay. The Michaelis constant (KM) value for ferricyanide was 0.86 mM. The enzyme’s half-life of deactivation at 45 °C was 12.3 min. The enzyme was most active at pH 6. The enzyme’s preferred substrate is 1-chloro-2, 4-dinitrobenzene.
關聯: 135(4)
URI: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/37730
显示于类别:[生命科學系] 期刊論文

文件中的档案:

档案 描述 大小格式浏览次数
index.html0KbHTML94检视/开启


在NTOUR中所有的数据项都受到原著作权保护.

 


著作權政策宣告: 本網站之內容為國立臺灣海洋大學所收錄之機構典藏,無償提供學術研究與公眾教育等公益性使用,請合理使用本網站之內容,以尊重著作權人之權益。
網站維護: 海大圖資處 圖書系統組
DSpace Software Copyright © 2002-2004  MIT &  Hewlett-Packard  /   Enhanced by   NTU Library IR team Copyright ©   - 回馈