Plant peroxidases were found to play an important role in plant physiology such as the metabolism and transformation of small complexes. In the present research, a novel Momordica charantia peroxidase (MCP) from fruits was purified to electrophoretic homogeneity by combining consecutive treatment of ammonium sulfate fractionation, ion exchange chromatography on DEAE-Sepharose FF, affinity chromatography on concanavalin A (Con A) Sepharose and gel filtration on Sephadex G-150. The physical and chemical characters of MCP were also investigated. MCP catalyzed the oxidation of ferulic acid (FA) to dehydrodimer (FA-2) in aqueous acetone system at pH 5.0. Its structure was identified by spectral analyses including IR, 1H-, 13C-NMR and electrospray ionization mass spectroscopy (ESI-MS). The anti-inflammatory activities of FA, FA-2 and other derivatives were examined. FA-2 significantly inhibited the release of proinflammatory factors such as TNF-alpha, NO and proliferation of spleen cells induced by phytohemagglutinin (PHA) and Con A and promoted a greater DNA fragmentation of spleen cells than that of other complexes. These results suggested that MCP as a tool enzyme transformed some complexes such as FA to more active derivatives, and that FA-2 was a potential inhibitor on inflammation through interference with immune response in the process of inflammation, which maybe was associated with apoptosis of immune related cells induced by FA-2.
