Protease inhibitors characterisation by SDS-PAGE and MALDI-TOF from and their modulation of macrophage immune-inflammatory properties.

This study describes the extraction and identification by electrophoretic and spectrometric techniques of protease inhibitor from the medicinal plant as well as investigates their immunomodulatory properties and cell viability. The tubers were subjected to protease inhibitor extractions and characterised using SDS-PAGE and MALDI-TOF. The protein extracts were assessed for activities trypsin inhibition stoichiometry, haemagglutinating, cell viability, NO and TNF-α production inhibition. Concerning the protease inhibitors analysis through SDS-PAGE, the results showed two bands with 11 and 24 kDa, and the MS analysis detected the ions more intense of 4276.795 and 8563.361 in the roasted protein extract. The IC of trypsin inhibition was 0.119 and 0.302 mg L in the roasted and crude tuber, respectively. The protease inhibitors extract from the roasted tubers showed a reduction in the production of NO and TNF-α at concentrations lower than 100 µg mL, without a reduction in cell viability.