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    STUDIA CHEMIA - Issue no. 2 / 2016  
         
  Article:   EXPRESSION AND PURIFICATION OF RECOMBINANT PHENYLALANINE AMMONIA-LYASE FROM PETROSELINUM CRISPUM.

Authors:  LÁSZLÓ CSABA BENCZE, LÁSZLÓ POPPE, CSABA PAIZS.
 
       
         
  Abstract:   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 KM, and kcat values suggesting excellent catalytic properties of the recombinant enzyme.

Keywords: phenylalanine ammonia-lyase, Petroselinum crispum, molecular cloning, expression and expression optimization
 
         
     
         
         
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