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A method for isolation of glutamin (asparagin) ase from Pseudomonas aurantiaca BKMB-548 has been developed. The enzyme preparation is homogeneous during polyacrylamide gel electrophoresis (pH 7.5 and 7.0) with SDS. The pH-optima of the enzyme thermal stability and of the glutaminase activity are equal to 6.0-8.0. At higher pH values the asparaginase activity increases within the pH range of 4-9. The amino acid composition of glutamin(asparagin)ase has been determined.
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