Abstract:Bovine β-casein (β-CN) with the C-terminal truncated by chymosin digestion, 1-192 fragment (β-CN-(f1-192)), was examined using circular dichroism (CD) under various temperature and solvent conditions. The effect of C-terminal deletion on the structure and stability of the parent protein, β -casein (β-CN), is analyzed and discussed. Analytical ultracentrifugation results showed reduced degree of self -association in β-CΝ-(f1-192) compared to whole β-casein. CONTIN/LL analysis of the CD data revealed clear chang… Show more
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