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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Bibliographic Details
Published inWater science & technology. Water supply Vol. 12; no. 3; pp. 329 - 333
Main Author SATHIYABAMA, M
Format Journal Article
LanguageEnglish
Published London International Water Association 01.01.2012
IWA Publishing
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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.
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