Journal
PROCESS BIOCHEMISTRY
Volume 44, Issue 4, Pages 504-508Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.procbio.2009.01.002
Keywords
Protein purification; Lectin; Moringa oleifera; Coagulant activity; Water treatment; Natural coagulants
Categories
Funding
- Conselho Nacional de Desenvolvimento Cientifico e Tecnologico (CNPq)
- Fundacao de Amparo A Ciencia e Tecnologia do Estado de Pernambuco (FACEPE)
- Coordenacao de Aperfeicoamento de Pessoal de Nivel Superior (CAPES)
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In this work hemagglutinating activity (HA) was investigated in distinct Moringa oleifera tissue extracts. A new lectin from seeds (cMoL) was purified and characterized; hemagglutinating and coagulating activities were evaluated. HA was detected in 0.15 M NaCl extracts from flowers and rachis inflorescence (5%, w/v), seeds, leaves, fundamental tissue of stem and steam bark (10%, w/v). cMoL isolated after saline extraction and guar gel column chromatography was active at pH range 4.0-9.0 agglutinating erythrocytes from rabbit and human blood types. Extracts of tissues and cMoL activities were carbohydrate inhibited; azocasein and asialofetuin abolished cMoL HA. The lectin was thermostable at 100 degrees C during 7 h. Polyacrylamide gel electrophoresis under reduced conditions revealed a main polypeptide band of 26.5 kDa; native basic cMoL was detected as a unique band. Seed lectin preparations and cMoL showed coagulant activity, similar to aluminium sulphate, the coagulant most widely used in water treatment. (C) 2009 Elsevier Ltd. All rights reserved.
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