Abstract
The mechanical behavior of films of milk proteins formed at the air-water interface has been determined. At the highest surface concentrations examined films of α s1 - and β-caseins showed no detectable viscosity, k-casein and α-lactalbumin gave viscous films, while the films of bovine serum albumin and β-lactoglobulin were viscoelastic. If the structure of k-casein was modified by cleaving and blocking the disulphide bonds, the resultant material formed films with no detectable surface viscosity. This observation is confirmed by experiments with indicator oils. The results suggest that globular proteins give films with a higher surface viscosity than those formed by random coil proteins. Qualitatively this can be explained in terms of the Moore and Eyring theory of surface viscosity.
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.
