Partial characterization of lectin of cassava leaves (Manihot esculenta Crantz).
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Partial characterization of lectin of cassava leaves (Manihot esculenta Crantz).
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| Id. |
33723477 |
| Idioma |
PT
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| Titulo |
Partial characterization of lectin of cassava leaves (Manihot esculenta Crantz). |
| Autor(es) |
Maria Cristina Silva
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| Localización |
http://bibtede.ufla.br/tede//tde_busca/arquivo.php?codArquivo=1078
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| Versión |
1.0 |
| Estado |
Final
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| Descripción |
Lectins are carbohydrates binding proteins (or glycoproteins) and owing to this property are capable of provoking agglutination of cells, mainly red blood cells (phenomenon known as hemagglutination). Are widely distributes in nature, found it in a number of organisms, since viruses and bacteria till animals and plants. Some of these proteins are toxic and or antinutritive and when ingested they incite adverse physiologic effects in the organism. Nevertheless, lectins awake the scientific interest, since they stand for important tools in research in the biologic and medical areas. Cassava leaf flour (FFM), a sub product of agricultural has been utilized as a food supplement for low income populations. Thus, the study of FFM lectin is extremely important both for its anti nutritional action and for its possible biotechnological applications, adding values to the sub products. The objective of this work was extracting, purifying and characterizing FFM lectin both its chemical and biological properties. For the extraction of FFM proteins, several extraction methods have been tested, in which two extractors were employed: distilled water and buffered saline solution (0.15mol L-1 NaCl, phosphate buffer pH 7.4) and four extraction times, 15, 60, 120 and 180 minutes. The extraction method which provided highest hemagglutinating activity (AH) was obtained when water was utilized as an extractor, in a time of 15 minutes (ratio 1:20 m/v). The FFM lectin file a thermal stability in a temperature range of 40 to 70º C and it is not dependent on Ca2+ and Mn2+ ions to exercise its AH. The protein extract was precipitated with ammonium sulfate at 80% of saturation and the precipitate was submitted to Sepharose CL-4B bio affinity column chromatography. Chromatography showed a peak which presented AH and when taken to polyacrylamide gel electrophoresis in the presence of SDS revealed three protein bands of 64, 61 and 58 kDa. The FFM?s protein extract that precipitated with ammonium sulfate at 80% of saturation don?t presented inhibitory effect don mycelial growth of the fungus Fusarium oxysporum, at the concentration of up to 100amp;#956;g mL-1.
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| Tipo |
PDF
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| Palabras clave |
BIOQUIMICA
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| Tipo de recurso |
Electronic Thesis or Dissertation
Tese ou Dissertacao Eletronica
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| Tipo de Interactividad |
Expositivo
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| Nivel de Interactividad |
muy bajo
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| Audiencia |
Estudiante
Profesor
Autor
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| Estructura |
Atomic |
| Coste |
no
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| Copyright |
sí
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Liberar o conteúdo dos arquivos para acesso público |
| Formatos |
PDF
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| Requerimientos técnicos |
Browser: Any
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| Fecha de contribución |
06-sep-2008 |
| Contacto |
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