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Elevated temperature and chemical modification selectively abolishes levan forming activity of levansucrase of Zymomonas mobilis

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Abstract

A levansucrase (SacB) of Zymomonas mobilis was purified to electrophoretic homogeneity from a recombinant Escherichia coli. The 55 kDa enzyme hydrolysed β-fructosides but not α-glucosides and catalysed levan formation from sucrose as well as raffinose. The optimum temperature for polymerase activity (30 °C ) was lower than that for hydrolase activity (50 °C ). In contrast to other levansucrases, polymerase activity of levansucrase was inhibited by para- chloromercuribenzoate (1 mM) but with little or no effect on hydrolase activity. Selective modulation of polymerase activity by this inhibitor will be useful in revealing the mechanism of levansucrase catalysis.

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Sangiliyandi, G., Chandra Raj, K. & Gunasekaran, P. Elevated temperature and chemical modification selectively abolishes levan forming activity of levansucrase of Zymomonas mobilis . Biotechnology Letters 21, 179–182 (1999). https://doi.org/10.1023/A:1005493024086

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  • DOI: https://doi.org/10.1023/A:1005493024086

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