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Specificity of maltase to maltose in three different directions of reaction: Hydrolytic, vanillyl alcohol glucoside and vanillyl alcohol isomaltoside synthesis

Authors

  • Aleksandra Dimitrijević,

    1. Faculty of Chemistry, Department of Biochemistry, University of Belgrade, Studentski trg 12, 11000 Belgrade, Serbia
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  • Dušan Veličković,

    Corresponding author
    1. Faculty of Chemistry, Department of Biochemistry, University of Belgrade, Studentski trg 12, 11000 Belgrade, Serbia
    • Faculty of Chemistry, Department of Biochemistry, University of Belgrade, Studentski trg 12, 11000 Belgrade, Serbia
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  • Nenad Milosavić,

    1. Faculty of Chemistry, Department of Biochemistry, University of Belgrade, Studentski trg 12, 11000 Belgrade, Serbia
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  • Dejan Bezbradica

    1. Faculty of Technology and Metallurgy, Department of Biochemical Engineering and Biotechnology, University of Belgrade, Karnegijeva 4, 11000 Belgrade, Serbia
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Abstract

Vanillyl alcohol glucoside is very attractive molecule due to its very powerful physiological activity. In this article, a detailed kinetic study of transglucosylation of vanillyl alcohol was performed. It was demonstrated that this reaction is very efficient (selectivity factor is 149) and occurred by a ping-pong mechanism with inhibition by glucose acceptor. At low concentration of vanillyl alcohol one additional transglucosylation product was detected. Its structure was determined to be α-isomaltoside of vanillyl alcohol, indicating that vanillyl alcohol glucoside is a product of the first transglucosylation reaction and a substrate for second, so the whole reaction mechanism was proposed. It was demonstrated that the rate of isomaltoside synthesis is two orders of magnitude smaller than glucoside synthesis, and that maltase has interestingly high Km value to maltose when vanillyl alcohol glucoside is second transglucosylation substrate. © 2012 American Institute of Chemical Engineers Biotechnol. Prog., 2012

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