Abstract
Differential centrifugation, precipitation with ammonium sulphate and chromatography on DEAE-cellulose led to a twenty-fold purification of glucosyltransferase fromStreptomyces aureofaciens B 96. The Michaelis constants for glucosyluridyl diphosphate (UDP-glucose) was 10.8 μm, for 1,2-dihydroxy-9, 10-anthraquinone (alizarin) 110 μm; the maximum rate of glucosylation reaction was 5.32 μmol per s per mg protein. The pH optimum was at 7.1; the flat temperature optimum was at 30 °C. Using some hydroxy derivatives of 9,10-anthraquinone it was found that the production of glucosides from aglycones with α-hydroxyl groups was about 1/8 of the values obtained with β-hydroxyl substrates. In both types of aglycones the presence of another hydroxyl group led to a higher glucoside production.
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Matějů, J., Cudlín, J., Steinerová, N. et al. Partial purification and properties of glucosyltransferase fromStreptomyces aureofaciens . Folia Microbiol 24, 205–210 (1979). https://doi.org/10.1007/BF02926449
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DOI: https://doi.org/10.1007/BF02926449