Artículo

Self-association of caseinomacropeptide in presence of CaCl2 at neutral pH: Calcium binding determination

Loria, Karina GabrielaIcon ; Pilosof, Ana Maria RenataIcon ; Farías, María Edith
Fecha de publicación: 03/2022
Editorial: Elsevier Science
Revista: LWT - Food Science and Technology
ISSN: 0023-6438
Idioma: Inglés
Tipo de recurso: Artículo publicado
Clasificación temática:

Resumen

The caseinomacropeptide (CMP) is a bioactive peptide produced during cheese making. It is found in abundancein whey. CMP aqueous solutions allow the incorporation of large amounts of CaCl2 but the mechanism of calcium-CMP interactions are unknown. In order to evaluate its calcium binding capacity, the following techniqueswere performed: Dynamic Light Scattering (DLS), Fourier Transform Infrared spectroscopy (FTIR), dialysis, conductivity,precipitation of CaCl2/CMP complex by ethanol, electrochemical Ca2+ binding isotherms, and inhibitionof calcium phosphate precipitation. One mole of CMP can bind 9 mol of calcium, and the CMP selfassemblesas a hexameric form. A model is proposed to explain the CMP self-association in presence of CaCl2.
Palabras clave: caseinimacropeptido , autoasociacion
 
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info:eu-repo/semantics/openAccess Excepto donde se diga explícitamente, este item se publica bajo la siguiente descripción: Creative Commons Attribution-NonCommercial-ShareAlike 2.5 Unported (CC BY-NC-SA 2.5)
Identificadores
URI: http://hdl.handle.net/11336/241608
URL: https://www.sciencedirect.com/science/article/pii/S0023643822003541
DOI: http://dx.doi.org/10.1016/j.lwt.2022.113419
Colecciones
Articulos(ITAPROQ)
Articulos de INSTITUTO DE TECNOLOGIA DE ALIMENTOS Y PROCESOS QUIMICOS
Citación
Loria, Karina Gabriela; Pilosof, Ana Maria Renata; Farías, María Edith; Self-association of caseinomacropeptide in presence of CaCl2 at neutral pH: Calcium binding determination; Elsevier Science; LWT - Food Science and Technology; 161; 3-2022; 1-8
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