HEXOSE OXIDATION BY AN ENZYME SYSTEM OF MALLEOMYCES PSEUDOMALLEI

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Abstract
Preparation and partial purification of a hexose oxidase from the pathogen M. pseudomallei is described. Oxidation of glucose and galactose to their corresponding hexonic acids was determined. In the case of galactose, absence of a demonstrable "galacto-waldenase" reaction was noted. The enzyme preparation differs from others described in that oxidation of the above substrates beyond gluconate or galactonate does not occur. The complete system can be precipitated by (NH4)2SO4 and purified further with MnCl2 or protamine sulfate. The enzyme system is not stimulated by added adenosinetriphosphate, diphosphopyridine nucleotide, triphospho pyridine nucleotide or Mg++. L-allose, L-altrose, D-arabinose, D-fructose, D-fructose-6-phosphate, D-fructose-1, 6-diphosphate, D-gulose, D-mannese-D-ribose, D-talose, D-xylose, malate, fumarate, alpha-keto-glutarate, glycerol, lactate, oxalacetate, acetate, citrate, pyruvate and succinate are not oxidized by the enzyme preparation. A modified procedure for disrupting bacterial cells by grinding in the Waring Blendor is described.