Submitted to: Meeting Abstract
Publication Type: Abstract Only
Publication Acceptance Date: June 4, 2004
Publication Date: July 16, 2004
Citation: Qi, P.X., Wickham, E. 2004. (The importance of the C-terminal region of bovine B-casein in its self-association behavior. (abstract). 228th ACS Natl. Mtg. Paper No. AGFD 56. Technical Abstract: The unique association behavior of beta-casein (beta-CN) makes it an important milk protein in the food industry, especially as a foaming and emulsifying agent. The effect of C-terminal deletion (193-209) on the temperature dependent self-association behavior of beta-CN was studied. Analytical ultracentrifugation results indicated significant reduction of self-association of beta-CN-(f1-192) compared to native beta-CN. Analysis of circular dichroism (CD) spectra revealed difference in temperature effect on the secondary structures of the two proteins. Binding of the fluorescence probe 1,8-ANS to beta-CN-(f1-192) was also significantly lower relative to beta-CN, suggesting a less open overall tertiary structure brought about by the C-terminal truncation. The results demonstrate that the tail peptide (193-209) is essential in maintaining the hydrophobic core of beta-CN and may further implicate its crucial role in the formation and stabilization of casein micelles.