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

Overview

Journal Food Technol Biotechnol

Specialty Biotechnology

Date 2016 Dec 14

PMID 27956861

Citations 7

Authors

Seda Sirin

Selcen Babaoglu Aydas

Belma Aslim

Affiliations

Soon will be listed here.

Abstract

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 -cinnamic acid. We assessed the PAL enzyme of the endemic plant (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 buffer (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.

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