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Issue 6, 2019, Issue in Progress
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Biochemical characterization and biocatalytic application of a novel d-tagatose 3-epimerase from Sinorhizobium sp.

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Abstract

Sinorhizobium sp. D-tagatose 3-epimerase (sDTE) catalyzes the conversion of D-tagatose to D-sorbose. It also recognizes D-fructose as a substrate for D-allulose production. The optimal temperature and pH of the purified sDTE was 50 °C and 8.0, respectively. Based on the sDTE homologous model, Glu154, Asp187, Gln213, and Glu248, form a hydrogen bond network with the active-site Mn2+ and constitute the catalytic tetrad. The amino acid residues around O-1, -2, and -3 atoms of the substrates (D-tagatose/D-fructose) are strictly conserved and thus likely regulate the catalytic reaction. However, the residues at O-4, -5, and -6, being responsible for the substrate-binding, are different. In particular, Arg65 and Met9 were found to form a unique interaction with O-4 of D-fructose and D-tagatose. The whole cells with recombinant sDTE showed a higher bioconversion rate of 42.5% in a fed-batch bioconversion using D-fructose as a substrate, corresponding to a production of 476 g L−1 D-allulose. These results suggest that sDTE is a potential industrial biocatalyst for the production of D-allulose in fed-batch mode.

Graphical abstract: Biochemical characterization and biocatalytic application of a novel d-tagatose 3-epimerase from Sinorhizobium sp.

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Publication details

The article was received on 06 Dec 2018, accepted on 15 Jan 2019 and first published on 22 Jan 2019


Article type: Paper
DOI: 10.1039/C8RA10029B
RSC Adv., 2019,9, 2919-2927
  • Open access: Creative Commons BY-NC license
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    Biochemical characterization and biocatalytic application of a novel D-tagatose 3-epimerase from Sinorhizobium sp.

    Z. Zhu, C. Li, X. Liu, D. Gao, X. Wang, M. Tanokura, H. Qin and F. Lu, RSC Adv., 2019, 9, 2919
    DOI: 10.1039/C8RA10029B

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