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Please use this identifier to cite or link to this item: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/39253

Title: Characterization of a Recombinant L-Ribose Isomerase from Geodermatophilus obscurus DSM 43160 and Application of this Enzyme to the Production of L-Ribose from L-Arabinose
Authors: Xing-Guang Hung
Ming-Yuan Yu
Yu-Chun Chen
Tsuei-Yun Fang
Contributors: 國立臺灣海洋大學:食品科學系
Keywords: Geodermatophilus obscurus.
L-ribose isomerase
L-ribulose
L-arabinose isomerase
Date: 2015
Issue Date: 2016-11-30T07:48:43Z
Publisher: Journal of Marine Science and Technology
Abstract: ABSTRACT: L-Ribose isomerase (L-RI) catalyzes the aldose-ketose isomerization between L-ribose and L-ribulose. In this study, a putative L-RI gene of Geodermatophilus obscurus DSM 43160 was cloned by PCR into pET-15b and pET-21b, respectively. The cloned target gene was expressed in Escherichia coli. The recombinant N-His-tagged and C-His-tagged proteins exhibited L-RI activity. Both N- and C-His-tagged L-RIs were purified from cell-free extracts by metal-affinity and ionexchange chromatography. The purified N-His-tagged L-RI demonstrated its optimal activity at 30-40C and pH of 9 (in glycine-NaOH buffer). The enzyme was stable at pH 7-9 and more than 90% activity was retained after incubation at 40C for 2 h. Metal ions were not required for N-His-tagged L-RI activity to occur, but Hg2+ inhibited its activity completely. The conversion rates of L-arabinose to L-ribose by combining Thermoanaerobacterium saccharolyticum NTOU1 L-arabinose
isomerase and G. obscurus DSM43160 N-His-tagged L-RI at 30C and 40C were 15.9% and 12.5% (mol mol-1), respectively. Results obtained from this study suggest a potential application of this recombinant L-RI for the L-ribose production from L-arabinose.
Relation: 23(4)
URI: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/39253
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