A β-cyano-L-alanine (β-CNAla)-degrading enzyme in Pseudomonas sp. 13 was purified and isolated as a crystalline preparation. The purification procedure involved ethanol fractionation, ammonium sulfate fractionation, column chromatography on DEAE-cellulose and crystallization in the presence of ammonium sulfate, resulting in 660-fold purification with a yield of 21%.
The crystalline enzyme was homogeneous as judged by ultracentrifugation and SDS-polyacrylamide gel electrophoresis. The enzyme has a molecular weight of approximately 1, 000, 000, and consists of about 30 apparently identical subunits, each of a molecular weight of approximately 35, 000.
The enzyme catalyzed the hydrolysis of β-CNAla to form asparagine and aspartic acid. The enzyme reaction was inhibited strongly by thiol reagents.

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