|Title||A simple purification and activity assay of the coagulant protein from Moringa oleifera seed|
|Publication Type||Journal Article|
|Year of Publication||2005|
|Authors||Ghebremichael, KA, Gunaratna, KR, Henriksson, H, Brumer, H, Dalhammar, G|
|Type of Article||Article|
Use of extracts from Moringa oleifera (MO) is of great interest for low-cost water treatment. This paper discusses water and salt extraction of a coagulant protein from the seed, purification using ion exchange, its chemical characteristics, coagulation and antimicrobial properties. The coagulant from both extracts is a cationic protein with pI greater than 9.6 and molecular mass less than 6.5 kDa. Mass spectrometric analysis of the purified water extract indicated that it contained at least four homologous proteins, based on MS/MS peptide sequence data. The protein is thermoresistant and remained active after 5 h heat treatment at 95 degrees C. The coagulant protein showed both flocculating and antibacterial effects of 1.1-4 log reduction. With samples of high turbidity, the MO extract showed similar coagulation activity as alum. Cecropin A and MO extract were found to have similar flocculation effects for clay and microorganisms. Simple methods for both the purification and assay of MO coagulating proteins are presented, which are necessary for large-scale water treatment applications. (c) 2005 Elsevier Ltd. All rights reserved.