| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 34155 | Process Biochemistry | 2016 | 7 Pages |
•A coagulant protein from M. oleifera seed extract was purified to a purity of 94%.•Purified MOCP was capable to aggregate bentonite colloids in aqueous solutions.•MOCP remained stable at 121 °C and 1.5 bar for at least 15 min.•MOCP is proposed to be an intrinsic disordered protein.
Coagulant proteins from Moringa oleifera (MO) seeds were successfully purified by removing seed oil followed by a protein salting out method at 40% (NH4)2SO4 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 °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 °C). The purified, thermo-stable coagulating protein retained its coagulating activity paving the way to economically produce a sterile natural coagulant from MO seeds.
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