Isolation and characterization of a flocculating protein from Moringa oleifera Lam.

U Gassenschmidt, K D Jany, B Tauscher, H Niebergall

Bundesforschungsanstalt für Ernährung, Karlsruhe Germany.

Biochimica et biophysica acta 1995 Apr 13

filter terms:

A flocculating protein from the seeds of Moringa oleifera Lam. was isolated by extraction with phosphate buffer followed by cation exchange chromatography. The molecular mass of the protein determined by SDS-PAGE was about 6.5 kDa, the isoelectric point was above pH 10. Amino acid analysis and sequencing showed high contents of glutamine, arginine and proline, and a total of 60 residues. The amino terminus is blocked by pyroglutamate. The flocculant capacity, determined in glass powder suspension, is comparable to that of a cationic polymer on polyacrylamide basis. Flocculation activity may be explained by the patch charge mechanism due to low molecular weight and high charge density.

Citation

U Gassenschmidt, K D Jany, B Tauscher, H Niebergall. Isolation and characterization of a flocculating protein from Moringa oleifera Lam. Biochimica et biophysica acta. 1995 Apr 13;1243(3):477-81