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

  • Selim M
  • Karm Eldin E
  • Saad M
  • et al.
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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.

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Selim, M. H., Karm Eldin, E.-Z., Saad, M. M., Mostafa, E.-S. E., Shetia, Y. H., & Anise, A. A. H. (2015). Purification, Characterization of L-Methioninase from Candida tropicalis , and Its Application as an Anticancer . Biotechnology Research International, 2015, 1–10. https://doi.org/10.1155/2015/173140

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