Your browser doesn't support javascript.
loading
Characterization of casein micelle precipitation by chitosans.
Ausar, S F; Bianco, I D; Badini, R G; Castagna, L F; Modesti, N M; Landa, C A; Beltramo, D M.
Afiliação
  • Ausar SF; Centro de Excelencia en Productos y Procesos de Córdoba (CEPROCOR) Agencia Córdoba Ciencia S.E., Pabellón CEPROCOR, Santa Maria de Punilla, Argentina.
J Dairy Sci ; 84(2): 361-9, 2001 Feb.
Article em En | MEDLINE | ID: mdl-11233020
We have found that the addition of chitosan, a cationic polymer, on whole or skim milk produces destabilization and coagulation of casein micelles that takes place without changes in the milk pH or the stability of most whey proteins. The amount of lipids recovered in the chitosan-casein aggregates was similar or higher than that obtained with rennet or acid precipitation. Approximately 70% of milk Ca2+ (approximately 750 mg/L) was found in the chitosan-induced aggregates, which is 10 and 50% higher than the amounts observed with acid or rennet coagulations, respectively. Purified alpha, beta-, and kappa-caseins were extensively precipitated by different molecular weight chitosans at pH 6.8. The phosphate groups of caseins seem not to be relevant in this interaction because dephosphorylated alpha- and beta-caseins were equally precipitated with chitosans. Analysis by optical microscopy of the chitosan-casein complex reveals that the size of the aggregates increase as the molecular weight of chitosans increase. Hydrophobic and electrostatic interactions particpate in the association and coagulation of casein micelles with chitosans of different molecular weights. The phenomenon is observed over a broad range of temperature (4 to 70 degrees C) with a reduction in the concentration of chitosan needed to precipitate the caseins that parallels a reduction in the viscosity of the chitosan solutions. Taken together, the results indicate that the electrostatic interactions may contribute energetically to the association between the two biopolymers, but the hydrophobicity of the complex would be the key determinant in the overall energetics of the reaction.
Assuntos
Buscar no Google
Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Caseínas / Quitina / Leite / Micelas Limite: Animals Idioma: En Revista: J Dairy Sci Ano de publicação: 2001 Tipo de documento: Article País de afiliação: Argentina País de publicação: Estados Unidos
Buscar no Google
Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Caseínas / Quitina / Leite / Micelas Limite: Animals Idioma: En Revista: J Dairy Sci Ano de publicação: 2001 Tipo de documento: Article País de afiliação: Argentina País de publicação: Estados Unidos