Expression and Purification of Recombinant Phenylalanine Ammonia-Lyase from Petroselinum Crispum

In the present study the molecular cloning, expression and purification of recombinant PcPAL, with a cleavable N-terminal His-tag is described. The PcPAL gene was cloned into pET-19b vector and transformed to different E. coli host cells. The optimization of expression and purification processes provided recombinant protein with high purity in its native, tetrameric fold with a yield of 7-8 mg protein / 1 L culture. The activity of the recombinant protein was tested towards its natural substrate L-Phe, the K-M, and k(cat) values suggesting excellent catalytic properties of the recombinant enzyme.