A coagulant protein from seeds of Moringa concanensis was isolated and purified using CM-Sepharose column chromatography. The column matrix was equilibrated with ammonium acetate buffer and maximum protein was eluted at 0.8 M NaCl. The molecular mass of the purified protein was identified as 14 kDa and its pI value was around 9.5. The purified coagulant protein retained 90% coagulation activity even after incubation at 90 °C for 3 h. The purified protein does not release organic content to the water. This paper suggests that coagulant protein from M. concanenesis can be used in drinking water treatment.

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