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- W2099682472 abstract "Gene araA encoding an l-arabinose isomerase (AraA) from the hyperthermophile, Thermotoga neapolitana 5068 was cloned, sequenced, and expressed in Escherichia coli. The gene encoded a polypeptide of 496 residues with a calculated molecular mass of 56 677 Da. The deduced amino acid sequence has 94.8% identical amino acids compared with the residues in a putative l-arabinose isomerase of Thermotoga maritima. The recombinant enzyme expressed in E. coli was purified to homogeneity by heat treatment, ion exchange chromatography and gel filtration. The thermophilic enzyme had a maximum activity of l-arabinose isomerization and d-galactose isomerization at 85°C, and required divalent cations such as Co2+ and Mn2+ for its activity and thermostability. The apparent Km values of the enzyme for l-arabinose and d-galactose were 116 mM (vmax, 119 μmol min−1 mg−1) and 250 mM (vmax, 14.3 μmol min−1 mg−1), respectively, that were determined in the presence of both 1 mM Co2+ and 1 mM Mn2+. A 68% conversion of d-galactose to d-tagatose was obtained using the recombinant enzyme at the isomerization temperature of 80°C." @default.
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- W2099682472 date "2002-06-01" @default.
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- W2099682472 title "Cloning, expression and characterization of l-arabinose isomerase from<i>Thermotoga neapolitana</i>: bioconversion of d-galactose to d-tagatose using the enzyme" @default.
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- W2099682472 doi "https://doi.org/10.1111/j.1574-6968.2002.tb11254.x" @default.
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