getpdf  NLM-PubMed-Logo  doi: 10.17113/ftb. 

Biochemical Evaluation of Phenylalanine Ammonia Lyase from Endemic Plant Cyathobasis fruticulosa (Bunge) Aellen. for the Dietary Treatment of Phenylketonuria

Seda Şirin1*, Selcen Babaoğlu Aydaş2 and Belma Aslım1

1Gazi University, Faculty of Science, Department of Biology, TR-06500 Teknikokullar, Ankara, Turkey
2Gazi University, Vocational High School of Health Services, TR-06830 Gölbaşı, Ankara, Turkey

Article history: 
Received November 2, 2015
Accepted April 12, 2016

Key words:
Cyathobasis fruticulosa, endemic plant, enzyme purifi cation, phenylalanine ammonia lyase (PAL), phenylketonuria (PKU)


Enzyme substitution therapy with the phenylalanine ammonia lyase (PAL) is a new approach to the treatment of patients with phenylketonuria (PKU). This enzyme is responsible for the conversion of phenylalanine to trans-cinnamic acid. We assessed the PAL enzyme of the endemic plant Cyathobasis fruticulosa (Bunge) Aellen. for its possible role in the dietary treatment of PKU. The enzyme was found to have a high activity of (64.9±0.1) U/mg, with the optimum pH, temperature and buff er (Tris–HCl and l-phenylalanine) concentration levels of pH=8.8, 37 °C and 100 mM, respectively. Optimum enzyme activity was achieved at pH=4.0 and 7.5, corresponding to pH levels of gastric and intestinal juice, and NaCl concentration of 200 mM. The purification of the enzyme by 1.87-fold yielded an activity of 98.6 U/mg. PAL activities determined by HPLC analyses before and after purification were similar. Two protein bands, one at 70 and the other at 23 kDa, were determined by Western blot analysis of the enzyme. This enzyme is a potential candidate for serial production of dietary food and biotechnological products.


*Corresponding author:  email3
                                      tel3  +90 312 202 1207
                                      fax2  +90 0312 212 2279

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