Purification of a coagulant protein from seeds of Moringa concanensis
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...
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Published in | Water science & technology. Water supply Vol. 12; no. 3; pp. 329 - 333 |
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Main Author | |
Format | Journal Article |
Language | English |
Published |
London
International Water Association
01.01.2012
IWA Publishing |
Subjects | |
Online Access | Get full text |
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Summary: | 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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Bibliography: | ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 |
ISSN: | 1606-9749 1607-0798 |
DOI: | 10.2166/ws.2011.140 |