Abstract
Functional properties of casein isolated by UF and cryodestabilization as compared with commercial caseinates were assessed. Cryocasein was readily resuspended in water by the application of agitation and mild heat. Solubility profiles of cryocasein suggested a partial disintegration of micellar structure by the changes in pH and ionic strength. In spite of its resuspendibility, the emulsifying properties of cryocasein were not as good as those of commercial caseinates. Cryocasein retained the ability of native casein micelles in milk to form a curd upon rennet addition. It formed a firmer gel with a lower syneresis than sodium caseinate and calcium caseinate with added 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.
