<p>Some proteins can be used as carriers for certain polyphenols (such as curcumin) to address the issue of their low bioavailability and to develop novel functional foods. As a result, one of the purposes of this review is to provide a brief overview of polyphenol carrier proteins. Bovine serum albumin (BSA), in particular, has the potential to become an ideal carrier material for curcumin encapsulation. Thus, for the possible use of curcumin-loaded BSA particles to reduce breast cancer incidence, an assessment of the impact of BSA particle size and curcumin concentration at pH 7 on curcumin encapsulation efficiency using BSA represents a valuable contribution to the BSA’s use as a delivery system for curcumin. This forms the main goal of this review. Hydrophobic interactions should play a relevant role in BSA-curcumin binding process such that, the main binding site on the BSA molecules for the curcumin molecules should be located inside a hydrophobic binding pocket of the BSA subdomain IIA near Trp₂₁₃. On the other hand, when account is taken only of the impact of pH conditions on the BSA particle physicochemical characteristics, the largest size of BSA particles should correspond to BSA isoelectric point, and the larger the size of BSA particles, the higher the curcumin encapsulation efficiency. In addition to BSA particle size, curcumin concentration has a strong influence on the efficiency of its encapsulation. However, BSA particle size and curcumin-to-BSA ratio should be optimized for the possible use of curcumin-loaded BSA particles to reduce breast cancer incidence.</p>