Table of Contents
Biotechnology Research International
Volume 2015, Article ID 173140, 10 pages
Research Article

Purification, Characterization of L-Methioninase from Candida tropicalis, and Its Application as an Anticancer

1National Research Centre, P.O. Box 12622, Dokki, Giza, Egypt
2Faculty of Science, Ain Shams University, Cairo, Egypt

Received 28 July 2015; Revised 10 October 2015; Accepted 13 October 2015

Academic Editor: Leandro Pena

Copyright © 2015 Mohsen Helmy Selim et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


The aim of the present study is to purify L-methioninase from Candida tropicalis 34.19-fold with 27.98% recovery after ion exchange chromatography followed by gel filtration. The purified enzyme revealed a single band on SDS-PAGE gel with a molecular weight of 46 KDa. Its optimum temperature was 45 to 55 and thermal stability was 55°C for 15 min. The enzyme had optimum pH at 6.5 and stability at a pH range of 5.5 to 7.0 for 24 hr. The maximum activity was observed with substrate concentration of 30 µM and Km was 0.5 mM. The enzyme was strongly inhibited by Cd+2 and Cu+2 while it was enhanced by Na+, Ni+2, and Mg+2 at 10 mM while Ca+2 had slight activation at 20 mM. In addition, the potential application of the L-methioninase as an anticancer agent against various types of tumor cell lines is discussed.