Isolation and characterization of a flocculating protein from Moringa oleifera Lam.
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.
Gassenschmidt
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U
Bundesforschungsanstalt für Ernährung, Karlsruhe Germany.
Jany
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KD
Tauscher
B
B
Niebergall
H
H
D000596:Amino Acids / Q000032:analysis; D002021:Buffers; D002852:Chromatography, Ion Exchange; D004563:Electrochemistry; D004591:Electrophoresis, Polyacrylamide Gel; D007526:Isoelectric Point; D008970:Molecular Weight; D010710:Phosphates; D010940:Plant Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification*; D012639:Seeds / Q000737:chemistry*; D017421:Sequence Analysis
D000596:Amino Acids; D002021:Buffers; D010710:Phosphates; D010940:Plant Proteins; C093273:flocculant protein MO 2.1, Moringa oleifera