PMID: 38193Jan 1, 1979

Partial purification and properties of glucosyltransferase from Streptomyces aureofaciens

Folia Microbiologica
J MatĕjůZ Vanĕk


Differential centrifugation, precipitation with ammonium sulphate and chromatography on DEAE-cellulose led to a twenty-fold purification of glucosyltransferase from Streptomyces aureofaciens B 96. The Michaelis constants for glucosyluridyl diphosphate (UDP-glucose) was 10.8 microM for 1,2-dihydroxy-9,10-anthraquinone (alizarin) 110 microM; the maximum rate of glucosylation reaction was 5.32 mumol per s per mg protein. The pH optimum was at 7.1; the flat temperature optimum was at 30 degrees C. Using some hydroxy derivatives of 9,10-anthraquinone it was found that the production of glucosides from aglycones with alpha-hydroxyl groups was about 1/8 of the values obtained with beta-hydroxyl substrates. In both types of aglycones the presence of another hydroxyl group led to a higher glucoside production.


Jan 1, 1978·Folia Microbiologica·J MatĕjůZ Vanĕk
Jan 1, 1977·Folia Microbiologica·J HorákL Ríhová
Jan 4, 1957·Science·M A JERMYN
Sep 1, 1957·Biochimica Et Biophysica Acta·J R FLORINI, C S VESTLING

Related Concepts

Streptomyces aureofaciens
Uridine Diphosphate Glucose
Hydrogen-Ion Concentration

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