Immobilization of l-methioninase on a zirconium-based metal–organic framework as an anticancer agent

Abstract

The development of new anticancer agents is very important, but challenging. Herein, a zirconium-based metal organic framework (UiO-66-COOH) was synthesized, and L-methioninase enzyme was purified from Wickerhamomyces subpelliculosus. Subsequently, a new composite (METase@UiO-66) was prepared from L-methioninase and UiO-66-(COOH). The METase@UiO-66 composite was characterized via scanning electron microscopy analysis and powder X-ray diffraction analysis. Moreover, the effects of pH, temperature and storage stability on the composite were well studied. The interesting results revealed greater stability of the composite as compared to that of the free enzyme. The composite was stable at 80 °C for around 40 minutes, and it showed better tolerance to variation in the reaction pH (5–7). Moreover, the storage stability of METase was significantly improved after immobilization, and the composite retained its full activity even after 12 days at 4 °C. In addition to the immobilization of the enzyme onto an MOF, the anti-cancer activity of the composite was investigated. For the first time, this composite was tested for the treatment of mice-bearing tumors, and the results of the in vivo studies showed that the treatment of mice-bearing tumors with the METase@UiO-66 composite caused a marked inhibition of tumor growth. Thus, the advantages of the METase@UiO-66 composite make it a promising anticancer agent in the field of cancer treatment.