Crystallization and properties of L-phenylalanine ammonia-lyase from Rhodosporidium toruloides.

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Abstract
L-Phenylalanine ammonia-lyase was crystallized for the first time from a cell-free extract of Rhodosporidium toruloides IFO 0559. Heat treatment at 50°C for 5min was a smart step for enzyme purification. Column chromatographies with DEAE-cellulose and hydroxyapatite, and gel filtration on a Sephadex G-200 column were used in the subsequent purification. The enzyme was purified to a homogeneous state and crystallized as fine needles with ammonium sulfate. The crystalline enzyme was pure by both analytical ultracentrifugation and polyacrylamide gel electrophoresis. The enzyme had a 8.2 s sedimentation velocity. The molecular weight of the enzyme was 165, 000 by the dual methods of sedimentation equilibrium and gel filtration. The enzyme was composed of two identical subunits with a molecular weight of 80, 000.

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