Binding affinity of curcumin to bovine serum albumin enhanced by pulsed electric field pretreatment

The present study investigated the effect of pulsed electric field (PEF) pretreatment on the interaction between bovine serum albumin (BSA) and curcumin. Fluorescence quenching results showed that proper PEF pretreatment significantly increased the binding affinity of curcumin and BSA, the binding constant increased by 6.77 times under the conditions of 15 kV/cm for 0.51 ms. However, at higher PEF strength (>= 25 kV/cm) and longer processing time (>= 0.68 ms), the binding affinity was weakened. PEF pretreatment made the protein structure more disordered and induced partial unfolding of BSA, exposing more hydrophobic regions, thereby increasing the binding affinity to curcumin. PEF-treated BSA (PBSA) possessed better encapsulation efficiency (95.19%) and loading capacity (5.25 mg/g) for curcumin, and the storage stability of curcumin were enhanced by the formation of a complex with PBSA. This study provides new insights into the design of BSA-based delivery systems for curcumin and other hydrophobic nutrients.

Automated summary

This study found that pulsed electric field pretreatment can increase the binding affinity between curcumin and bovine serum albumin, and improve the loading capacity and storage stability of curcumin. PEF pretreatment makes the protein structure more disordered and increases the binding affinity to curcumin.