Purification of phenylalanine ammonia lyase from Rhodotorula glutinis

A simple and rapid method employing four steps; sonication, salt precipitation, gel filtration on Sephacryl-S-400 followed by hydrophobic interaction chromatography on Phenyl Sepharose CL-4B for the purification of phenylalanine ammonia lyase from the yeast Rhodotorula glutinis is described. The preparation gave an overall yield of 33%, 195-fold purification and a high specific activity of 4.69 U mg(-1) protein. The final preparation was homogeneous as judged from native polyacrylamide gel electrophoresis.