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Please use this identifier to cite or link to this item: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/39255

Title: Characterization of a Thermophilic L-Arabinose Isomerase from Thermoanaerobacterium saccharolyticum NTOU1
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: Thermophiles
Arabinose isomerase
Bioconversion
Recombinant DNA
Enzyme activity
Thermoanaerobacterium saccharolyticum
Date: 2014-02
Issue Date: 2016-11-30T07:56:29Z
Publisher: Biochemical Engineering Journal
Abstract: Abstract: l-Arabinose isomerase (EC 5.3.1.4, l-AI) mainly catalyzes the reversible aldose–ketose isomerization between l-arabinose and l-ribulose. l-AIs can also catalyze other reactions, such as the conversion of d-galactose to d-tagatose. In this study, the araA gene encoding l-AI was PCR-cloned from Thermoanaerobacterium saccharolyticum NTOU1 and then expressed in Escherichia coli. The recombinant l-AI was purified from the cell-free extract using nickel nitrilotriacetic acid metal-affinity chromatography. The purified enzyme showed an optimal activity at 70 °C and pH 7–7.5. The enzyme was stable at pHs ranging from 6.5 to 9.5 and the activity was fully retained after 2 h incubation at 55–65 °C. The low concentrations of divalent metal ions, either 0.1 mM Mn2+ or 0.05 mM Co2+, could improve both catalytic activity and thermostability at higher temperatures. The recombinant T. saccharolyticum NTOU1 l-AI has the lowest demand for metal ions among all characterized thermophilic l-AIs. This thermophilic l-AI shows a potential to be used in industry to produce d-tagatose from d-galactose.
Relation: 83
URI: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/39255
Appears in Collections:[食品科學系] 期刊論文

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