Purification and properties of glutaminase from Aspergillus oryzae |
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Affiliation: | 1. Neurology Laboratory, School of Health Sciences, Faculty of Medicine, University of Crete, Heraklion, Crete, Greece;2. Department of Molecular Pharmacology, Albert Einstein College of Medicine, Bronx, New York, USA |
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Abstract: | Glutaminase activity was found in a water extract of a wheat bran koji (extracellular fraction) of Aspergillus oryzae strains Lee-1, H-16 and MA-27-IM isolated from a commercial koji ssed for soy sauce fermentation, as well as in thier mycelia (intracellular fraction). Both the intracellular and the extracellular glutaminases were purified from strain MA-27-IM. Polyacrylamide gel electrophoresis of each purified preparation gave a single band with identical electrophoretic mobility. The molecular weight of the intracellular and the extracellular glutaminases were estimated to be approximately 113, 000. Both preparations hydrolyzed various γ-glutamyl compounds besides l-glutamine but did not exhibit asparaginase activity. Further investigation of these preparations inidicated that these glutaminases possessed almost the same properties, suggesting their similarity. |
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