PRODUCTION, OPTIMIZATION AND PURIFICATION OF L-METHIONINASE FROM Aspergillus flavipes AUMC 1201

L-methioninase (L-methionine-α-deamino-c-mercaptome-thane-lyase) (E.C 4.4.1.11) had received much attention for its importance as a drug target for many infectious diseases and for therapeutic interventions of various cancers. Therefore, the present study aimed to produce, optimize and purify extracellular L-methioninase from Aspergillus flavipes AUMC 1201. Enhanced production of L-methioninase occurred on the addition of 1.5% (w/v) glucose, 0.5% (w/v) L-methionine. Its optimum temperature was 30°C and the optimum pH was 8.0 for 8 days of shaking fermentation at 130 rpm. Purification fold of L-methioninase was 14.5 with 37.1% recovery after ammonium sulphate precipitation (90%), ion exchange chromatography on DEAE cellulose followed by gel filtration on Sephadex G-200. The purified enzyme revealed a single band on SDS-PAGE electrophoresis with a molecular weight of 48 KDa. Overall, purified L-methioninase can be used for further clinical applications.