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Título
effects of temperature, pH and sugar binding on the structures of lectins ebulin f and selfd
Año del Documento
2017
Editorial
Elsevier
Descripción
Producción Científica
Documento Fuente
Food Chemsitry, 2017,Volume 220, Pages 324-330
Abstract
Ebulin f and SELfd are two lectins of Sambucus ebulus L. that show different stability and digestibility properties in gastric fluid due to their structural differences which may explain their different toxicological profiles. The main aim was to determine the effects of pH, temperature and sugar binding on the intrinsic structures of both proteins by fluorescence analyses. Quenching experiments were conducted, under different pH and temperature conditions, with acrylamide (uncharged) and iodide (charged), to study the possible changes of their intrinsic fluorescence. Results revealed that the native structure of SELfd is more folded than that of ebulin f. At pH 2.0, ebulin f displayed a more open structure than at neutral pH. It can be concluded that this is the main reason why ebulin f is accessible to pepsin action and more sensitive to degradation, in contrast to SELfd as we reported previously.
Palabras Clave
Ebulin f
SELfd
Pepsin
Lactose
D-galactose
Lectin
Sambucus ebulus
Dwarf elder
ISSN
0308-8146
Revisión por pares
SI
Patrocinador
Grupo de Excelencia GR106
UVa-GIR Inmunotoxinas Antitumorales
Convenio Consejería de Sanidad JCyL
UVa-GIR Inmunotoxinas Antitumorales
Convenio Consejería de Sanidad JCyL
Version del Editor
Propietario de los Derechos
© Elsevier Ltd
Idioma
eng
Tipo de versión
info:eu-repo/semantics/acceptedVersion
Derechos
openAccess
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