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Isolation And Characterization Of Papain-Like Cysteine Proteinases From Morinda Citrifolia Seed With Anti-Toxoplasmose Effect

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Morinda citrifolia, known as Noni, is used in folk medicine with several therapeutic applications. The present study investigated the enzymatic and biological characteristics of the papain-like cysteine proteases (PLCP) from M. citrifolia seed. Its enzyme was purified in two-step by DEAE-Sephacel and Phenyl-Sepharose CL-4B (10 × 0.6 cm) columns. PLCP enzyme demonstrated an apparent molecular mass of 51 kDa on SDS-PAGE 14%. The proteolytic activity in the presence of fibrinogen with the PLPC of M. citrifolia demonstrated total hydrolysis of the fibrinogen chains, occurring in the concentration of 20 μg; with the optimum pH of 7.0; temperatures range from room temperature to 50°C; better activity with calcium ions and the effect of inhibition appeared in the presence of Leupeptin. There was no platelet aggregation or coagulation activity. PLCP enzyme was not cytotoxic for cells such as Human Foreskin Fibroblasts (HFF) and murine embryo fibroblasts strain NIH/Swiss (NIH/3T3) macrophages and showed to be effective when tested directly against Toxoplasma gondii infection in vitro. In that sense, this study indicates perspectives for pharmacological applications of M. citrifolia enzymes.

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Morinda citrifolia, Cysteine protease, proteolytic activity, Toxoplasma gondii

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MOTA, Danielly Christine Adriani Maia. Isolation and characterization of papain-like cysteine proteinases from Morinda citrifolia seed with anti-toxoplasmose effect. 2017. 23 f. Trabalho de Conclusão de Curso (Graduação em Biomedicina) - Faculdade de Ciências Biomédicas, Universidade Federal de Uberlândia. Uberlândia, 2017.

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