Coagulant proteins from Moringa oleifera (MO) seeds were successfully purified by removing seed oil followed by a protein salting out method at 40% (NH4)(2)SO4 combined with subsequent dialysis and heat treatment. A microtiter plate-based coagulation activity assay was then performed using colloidal bentonite solution and alum as positive control. The results, show an oil recovery of 40 +/- 2% while the water-soluble protein fraction in the defatted MO seed was 12.5 +/- 0.5 mg/g or 4.4% of the total seed protein content. Heating the desalted protein fraction to 121 degrees C helped to obtain a 94% pure protein of approximately 7 kDa. Computational analyses support the hypothesis that the coagulating MO protein is an intrinsically disordered protein, providing reason for its stability at extreme temperatures (121 degrees C). The purified, thermo-stable coagulating protein retained its coagulating activity paving the way to economically produce a sterile natural coagulant from MO seeds. (C) 2016 Elsevier Ltd. All rights reserved.