National Taiwan Ocean University Institutional Repository:Item 987654321/27405
English  |  正體中文  |  简体中文  |  全文笔数/总笔数 : 28611/40652
造访人次 : 783309      在线人数 : 58
RC Version 4.0 © Powered By DSPACE, MIT. Enhanced by NTU Library IR team.
搜寻范围 进阶搜寻


题名: Characterization of a Thermophilic l-Rhamnose Isomerase from Thermoanaerobacterium saccharolyticum NTOU1
作者: Chia-Jui Lin;Wen-Chi Tseng;Tien-Hsiang Lin;Shiu-Mei Liu;Wen-Shyong Tzou;Tsuei-Yun Fang
贡献者: NTOU:Department of Food Science
关键词: l-Rhamnose isomerase;d-allose;thermophilic enzyme;Thermoanaerobacterium saccharolyticum NTOU1;E. coli;overexpression
日期: 2010
上传时间: 2011-10-21T02:25:12Z
出版者: Journal of Agricultural and Food Chemistry
摘要: Abstract:l-Rhamnose isomerase (EC, l-RhI) catalyzes the reversible aldose−ketose isomerization between l-rhamnose and l-rhamnulose. In this study, the l-rhi gene encoding l-RhI was PCR-cloned from Thermoanaerobacterium saccharolyticum NTOU1 and then expressed in Escherichia coli. A high yield of the active l-RhI, 9780 U/g of wet cells, was obtained in the presence of 0.2 mM IPTG induction. l-RhI was purified sequentially using heat treatment, nucleic acid precipitation, and anion-exchange chromatography. The purified l-RhI showed an apparent optimal pH of 7 and an optimal temperature at 75 °C. The enzyme was stable at pH values ranging from 5 to 9, and the activity was fully retained after a 2 h incubation at 40−70 °C. l-RhI from T. saccharolyticum NTOU1 is the most thermostable l-RhI to date, and it has a high specific activity (163 U/mg) and an acceptable purity after heat treatment, suggesting that this enzyme has the potential to be used in rare sugar production.
關聯: 58(19), pp.10431–10436
显示于类别:[食品科學系] 期刊論文


档案 描述 大小格式浏览次数



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