RT info:eu-repo/semantics/article
T1 effects of temperature, pH and sugar binding on the structures of lectins ebulin f and selfd
A1 Carrillo, Celia
A1 Cordoba-Diaz, Damián
A1 Cordoba-Diaz, Manuel
A1 Girbés, Tomás
A1 Jiménez, Pilar
K1 Ebulin f
K1 SELfd
K1 Pepsin
K1 Lactose
K1 D-galactose
K1 Lectin
K1 Sambucus ebulus
K1 Dwarf elder
AB 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.
PB Elsevier
SN 0308-8146
YR 2017
FD 2017
LK https://uvadoc.uva.es/handle/10324/64332
UL https://uvadoc.uva.es/handle/10324/64332
LA eng
NO Food Chemsitry, 2017,Volume 220, Pages 324-330
NO Producción Científica
DS UVaDOC
RD 06-ago-2024