Isolation of a seed coagulant Moringa oleifera lectin
Main Author: | |
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Publication Date: | 2009 |
Other Authors: | , , , , |
Format: | Article |
Language: | eng |
Source: | Repositórios Científicos de Acesso Aberto de Portugal (RCAAP) |
Download full: | https://hdl.handle.net/1822/9494 |
Summary: | 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 °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. |
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Isolation of a seed coagulant Moringa oleifera lectinProtein purificationLectinMoringa oleiferaCoagulant activityWater treatmentNatural coagulantsScience & TechnologyIn 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 °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.Científico e Tecnológico (CNPq)Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)Fundação de Amparo à Ciência e Tecnologia do Estado de Pernambuco (FACEPE)ElsevierUniversidade do MinhoSantos, Andréa F. S.Luz, Luciana A.Argôlo, Adriana C. C.Teixeira, J. A.Paiva, Patrícia M. G.Coelho, L. C. B. B.2009-042009-04-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttps://hdl.handle.net/1822/9494eng"Process Biochemistry". ISSN 1359-5113. 44:4 (Apr. 2009) 504-508.1359-511310.1016/j.procbio.2009.01.002info:eu-repo/semantics/openAccessreponame:Repositórios Científicos de Acesso Aberto de Portugal (RCAAP)instname:FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologiainstacron:RCAAP2025-04-12T04:53:14Zoai:repositorium.sdum.uminho.pt:1822/9494Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireinfo@rcaap.ptopendoar:https://opendoar.ac.uk/repository/71602025-05-28T15:45:46.608460Repositórios Científicos de Acesso Aberto de Portugal (RCAAP) - FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologiafalse |
dc.title.none.fl_str_mv |
Isolation of a seed coagulant Moringa oleifera lectin |
title |
Isolation of a seed coagulant Moringa oleifera lectin |
spellingShingle |
Isolation of a seed coagulant Moringa oleifera lectin Santos, Andréa F. S. Protein purification Lectin Moringa oleifera Coagulant activity Water treatment Natural coagulants Science & Technology |
title_short |
Isolation of a seed coagulant Moringa oleifera lectin |
title_full |
Isolation of a seed coagulant Moringa oleifera lectin |
title_fullStr |
Isolation of a seed coagulant Moringa oleifera lectin |
title_full_unstemmed |
Isolation of a seed coagulant Moringa oleifera lectin |
title_sort |
Isolation of a seed coagulant Moringa oleifera lectin |
author |
Santos, Andréa F. S. |
author_facet |
Santos, Andréa F. S. Luz, Luciana A. Argôlo, Adriana C. C. Teixeira, J. A. Paiva, Patrícia M. G. Coelho, L. C. B. B. |
author_role |
author |
author2 |
Luz, Luciana A. Argôlo, Adriana C. C. Teixeira, J. A. Paiva, Patrícia M. G. Coelho, L. C. B. B. |
author2_role |
author author author author author |
dc.contributor.none.fl_str_mv |
Universidade do Minho |
dc.contributor.author.fl_str_mv |
Santos, Andréa F. S. Luz, Luciana A. Argôlo, Adriana C. C. Teixeira, J. A. Paiva, Patrícia M. G. Coelho, L. C. B. B. |
dc.subject.por.fl_str_mv |
Protein purification Lectin Moringa oleifera Coagulant activity Water treatment Natural coagulants Science & Technology |
topic |
Protein purification Lectin Moringa oleifera Coagulant activity Water treatment Natural coagulants Science & Technology |
description |
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 °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. |
publishDate |
2009 |
dc.date.none.fl_str_mv |
2009-04 2009-04-01T00:00:00Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
https://hdl.handle.net/1822/9494 |
url |
https://hdl.handle.net/1822/9494 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
"Process Biochemistry". ISSN 1359-5113. 44:4 (Apr. 2009) 504-508. 1359-5113 10.1016/j.procbio.2009.01.002 |
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info:eu-repo/semantics/openAccess |
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openAccess |
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application/pdf |
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Elsevier |
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Elsevier |
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