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

Abstract

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 µ M 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.