Abstract
The foaming properties of partially denatured α-lactalbumin was investigated. The partially denatured state was produced by removing bound Ca 2+ by treatment with ethylenediaminetetraacetic acid (EDTA) at pH 8.0 and 25°C. Surface tension measurements showed that partially denatured α-lactalbumin unfolds easily at liquid interfaces compared with the native protein. The results of foam volume and stability measurements were consistent with the results of surface tension measurements. In the presence of EDTA a considerable amount of foam was obtained at low concentrations, such as 0.1 mg/ml, and the foam stability was improved. This indicates the importance of the protein structure on the adsorption of molecules at liquid interfaces. The presence of Ca 2+ also resulted in an increase in the foamability and foam stability of α-lactalbumin compared with native protein, due to the saturation of the surface charges. This shows the binding affinity of protein to Ca 2+. The investigation of the effect of Ca 2+ on the surface behaviour of β-lactoglobulin, another whey protein, also showed an improvement in the foaming properties of protein.
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.
