Detection, purification and characterization of a lectin from freshwater green algae Spirogyra spp.

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Autor principal: ANTÔNIA S. DE OLIVEIRA
Formato: Artículo científico
Lenguaje:en
Publicado: Academia Brasileira de Ciências 2017
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author ANTÔNIA S. DE OLIVEIRA
author_facet ANTÔNIA S. DE OLIVEIRA
contents Detection, purification and characterization of a lectin from freshwater green algae Spirogyra spp. ANTÔNIA S. DE OLIVEIRA CLÁUDIA F. LÓSSIO ANNE J. RANGEL MARIA G.Q. MARTINS FERNANDO E.P. DO NASCIMENTO MARIA L.L. DE ANDRADE BENILDO S. CAVADA SÍRLEIS R. LACERDA KYRIA S. DO NASCIMENTO Multidisciplinaria (Ciencias Naturales y Exactas) Algae lectin purification characterization Freshwater algae are rich sources of structurally biologically active metabolites, such as fatty acids, steroids, carotenoids and polysaccharides. Among these metabolites, lectins stand out. Lectins are proteins or glycoproteins of non-immune origin which bind to carbohydrates or glycoconjugates, without changing ligand structure. Many studies have reported on the use of Spirogyra spp. as effective bioindicators of heavy metals; however, reports on Spirogyra molecular bioprospecting are quite limited. Therefore, this study aimed to detect, isolate, purify and characterize a lectin present in the freshwater green algae Spirogyra . Presence of the lectin protein in the extract was detected by hemagglutination assays. Subsequently, the protein extract was subjected to a sugar inhibition assay to identify the lectin-specific carbohydrate. Following this, the extract was applied to a guar gum column to afford the pure lectin. The lectin was inhibited by N-acetyl-glucosamine and N-acetyl-beta-D-mannose, but more strongly by D-galactose. The apparent molecular mass of the purified lectin was evaluated by Polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate (SDS-PAGE). Electrophoretic analysis revealed a single protein band with an apparent molecular mass of 56 kDa. Thus, it could be concluded that a lectin was purified from Spirogyra spp. 2017 artículo científico 0001-3765 https://www.redalyc.org/articulo.oa?id=32753602014 en http://www.redalyc.org/revista.oa?id=327 Anais da Academia Brasileira de Ciências application/pdf Academia Brasileira de Ciências Anais da Academia Brasileira de Ciências (Brasil) Num.3 Vol.89
format Artículo científico
id redalyc_32753602014
institution Redalyc
language en
publishDate 2017
publisher Academia Brasileira de Ciências
spellingShingle Detection, purification and characterization of a lectin from freshwater green algae Spirogyra spp.
ANTÔNIA S. DE OLIVEIRA
Multidisciplinaria (Ciencias Naturales y Exactas)
Algae
lectin
purification
characterization
Detection, purification and characterization of a lectin from freshwater green algae Spirogyra spp. ANTÔNIA S. DE OLIVEIRA CLÁUDIA F. LÓSSIO ANNE J. RANGEL MARIA G.Q. MARTINS FERNANDO E.P. DO NASCIMENTO MARIA L.L. DE ANDRADE BENILDO S. CAVADA SÍRLEIS R. LACERDA KYRIA S. DO NASCIMENTO Multidisciplinaria (Ciencias Naturales y Exactas) Algae lectin purification characterization Freshwater algae are rich sources of structurally biologically active metabolites, such as fatty acids, steroids, carotenoids and polysaccharides. Among these metabolites, lectins stand out. Lectins are proteins or glycoproteins of non-immune origin which bind to carbohydrates or glycoconjugates, without changing ligand structure. Many studies have reported on the use of Spirogyra spp. as effective bioindicators of heavy metals; however, reports on Spirogyra molecular bioprospecting are quite limited. Therefore, this study aimed to detect, isolate, purify and characterize a lectin present in the freshwater green algae Spirogyra . Presence of the lectin protein in the extract was detected by hemagglutination assays. Subsequently, the protein extract was subjected to a sugar inhibition assay to identify the lectin-specific carbohydrate. Following this, the extract was applied to a guar gum column to afford the pure lectin. The lectin was inhibited by N-acetyl-glucosamine and N-acetyl-beta-D-mannose, but more strongly by D-galactose. The apparent molecular mass of the purified lectin was evaluated by Polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate (SDS-PAGE). Electrophoretic analysis revealed a single protein band with an apparent molecular mass of 56 kDa. Thus, it could be concluded that a lectin was purified from Spirogyra spp. 2017 artículo científico 0001-3765 https://www.redalyc.org/articulo.oa?id=32753602014 en http://www.redalyc.org/revista.oa?id=327 Anais da Academia Brasileira de Ciências application/pdf Academia Brasileira de Ciências Anais da Academia Brasileira de Ciências (Brasil) Num.3 Vol.89
title Detection, purification and characterization of a lectin from freshwater green algae Spirogyra spp.
topic Multidisciplinaria (Ciencias Naturales y Exactas)
Algae
lectin
purification
characterization
url https://www.redalyc.org/articulo.oa?id=32753602014