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Core-shell particles formed by ß-lactoglobulin microgel coated with xyloglucan.
Gtari, Wala; Aschi, Adel; Nicolai, Taco; de Freitas, Rilton Alves.
Afiliação
  • Gtari W; Polymères, Colloïds, Interfaces, UMR CNRS Université du Maine, 72085 Le Mans Cedex 9, France; Université de Tunis El Manar, Faculté des Sciences de Tunis, LR99ES16 Laboratoire Physique de la Matière Molle et dela Modélisation Électromagnétique, 2092, Tunis, Tunisia.
  • Aschi A; Université de Tunis El Manar, Faculté des Sciences de Tunis, LR99ES16 Laboratoire Physique de la Matière Molle et dela Modélisation Électromagnétique, 2092, Tunis, Tunisia.
  • Nicolai T; Polymères, Colloïds, Interfaces, UMR CNRS Université du Maine, 72085 Le Mans Cedex 9, France.
  • de Freitas RA; Polymères, Colloïds, Interfaces, UMR CNRS Université du Maine, 72085 Le Mans Cedex 9, France; BioPol, Chemistry Department, Federal University of Paraná, 81531-980 Curitiba, PR, Brazil. Electronic address: rilton@quimica.ufpr.br.
Int J Biol Macromol ; 92: 357-361, 2016 Nov.
Article em En | MEDLINE | ID: mdl-27426701
ABSTRACT
Core-shell particles were formed by mixing in aqueous solution the neutral polysaccharide xyloglucan (XG) with microgels. The last one was obtained by heating the whey protein ß-lactoglobulin (ß-LG) in the presence of CaCl2. XG adsorbed spontaneously unto the microgels at pH<5.6. The amount of bound XG per protein was determined using a combination of centrifugation and size exclusion chromatography. It increased linearly with increasing XG concentration. The fraction of XG that adsorbed increased with decreasing pH. The formation of the XG shell inhibited large scale flocculation of the particles, that causes precipitation for naked microgels, close to their isoionic point. The thickness of the XG shell was estimated by measurement of the hydrodynamic radius using dynamic light scattering. The extent of binding depended on the pH history during mixing showing that the protein/XG complex was not in thermodynamic equilibrium.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Xilanos / Géis / Glucanos / Lactoglobulinas Idioma: En Revista: Int J Biol Macromol Ano de publicação: 2016 Tipo de documento: Article País de afiliação: Tunísia

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Xilanos / Géis / Glucanos / Lactoglobulinas Idioma: En Revista: Int J Biol Macromol Ano de publicação: 2016 Tipo de documento: Article País de afiliação: Tunísia