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Please use this identifier to cite or link to this item: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/27405

Title: Characterization of a Thermophilic l-Rhamnose Isomerase from Thermoanaerobacterium saccharolyticum NTOU1
Authors: Chia-Jui Lin;Wen-Chi Tseng;Tien-Hsiang Lin;Shiu-Mei Liu;Wen-Shyong Tzou;Tsuei-Yun Fang
Contributors: NTOU:Department of Food Science
國立臺灣海洋大學:食品科學系
Keywords: l-Rhamnose isomerase;d-allose;thermophilic enzyme;Thermoanaerobacterium saccharolyticum NTOU1;E. coli;overexpression
Date: 2010
Issue Date: 2011-10-21T02:25:12Z
Publisher: Journal of Agricultural and Food Chemistry
Abstract: Abstract:l-Rhamnose isomerase (EC 5.3.1.14, 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.
Relation: 58(19), pp.10431–10436
URI: http://ntour.ntou.edu.tw/handle/987654321/27405
Appears in Collections:[食品科學系] 期刊論文

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