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Properties of L-arabinose isomerase from Escherichia coli as biocatalyst for tagatose production

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Abstract

L-arabinose isomerase (EC 5.3.1.4) mediates the isomerization of D-galactose into D-tagatose as well as the conversion of L-arabinose into L-ribulose. To investigate the properties of L-arabinose isomerase as a biocatalyst for the conversion of galactose to tagatose, the L-arabinose isomerase of Escherichia coli was characterized. The substrate specificity for L-arabinose was 166-fold higher than that for D-galactose. The optimal pH and temperature for the galactose isomerization reaction were 8.0 and 30 °C, respectively. The enzyme activity was stable for 1 h at temperatures below 35 °C and within a pH range of 8–10. The Michaelis constant, K m, for galactose was 1480 mM, which is 25-fold higher than that for arabinose. The addition of Fe2+ and Mn2+ ions enhanced the conversion of galactose to tagatose, whereas the addition of Cu2+, Zn2+, Hg2+, and Fe3+ ions inhibited the reaction completely. In the presence of 1 mM Fe2+ ions, the K m for galactose was found to be 300 mM.

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Authors and Affiliations

  1. R&D Center, Tongyang Confectionery Co., Seoul, 140-715, Korea

    Sang-Hyun Yoon & Pil Kim

  2. Department of Bioscience and Biotechnology, Sejong University, 98 Gunja-dong, Gwangjin-gu, Seoul, 143-747, Korea; Tel.: +

    Deok-Kun Oh

Authors
  1. Sang-Hyun Yoon
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  2. Pil Kim
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  3. Deok-Kun Oh
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Yoon, SH., Kim, P. & Oh, DK. Properties of L-arabinose isomerase from Escherichia coli as biocatalyst for tagatose production. World Journal of Microbiology and Biotechnology 19, 47–51 (2003). https://doi.org/10.1023/A:1022575601492

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