Abstract
The caseinomacropeptide (CMP) is a bioactive peptide produced during cheese making. It is found in abundance in 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 techniques were performed: Dynamic Light Scattering (DLS), Fourier Transform Infrared spectroscopy (FTIR), dialysis, conductivity, precipitation of CaCl2/CMP complex by ethanol, electrochemical Ca2+ binding isotherms, and inhibition of calcium phosphate precipitation. One mole of CMP can bind 9 mol of calcium, and the CMP self-assembles as a hexameric form. A model is proposed to explain the CMP self-association in presence of CaCl2.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
