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

Rui Wang; Qin-Hui Wen; Xin-An Zeng; Jia-Wei Lin; Jian Li; Fei-Yue Xu

doi:10.1016/j.foodchem.2021.131945

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

Food Chem. 2022 May 30:377:131945. doi: 10.1016/j.foodchem.2021.131945. Epub 2021 Dec 24.

Authors

Rui Wang¹, Qin-Hui Wen², Xin-An Zeng³, Jia-Wei Lin¹, Jian Li¹, Fei-Yue Xu¹

Affiliations

¹ School of Food Science and Engineering, South China University of Technology, Guangzhou 510641, China; Overseas Expertise Introduction Center for Discipline Innovation of Food Nutrition and Human Health (111 Center), Guangzhou, China.
² School of Food Science and Engineering, South China University of Technology, Guangzhou 510641, China; Overseas Expertise Introduction Center for Discipline Innovation of Food Nutrition and Human Health (111 Center), Guangzhou, China; School of Chemistry, The University of Melbourne, Parkville, Victoria 3010, Australia.
³ School of Food Science and Engineering, South China University of Technology, Guangzhou 510641, China; School of Food Science and Engineering, Foshan University, Foshan 528000, China; Overseas Expertise Introduction Center for Discipline Innovation of Food Nutrition and Human Health (111 Center), Guangzhou, China. Electronic address: xazeng@scut.edu.cn.

PMID: 34999459
DOI: 10.1016/j.foodchem.2021.131945

Abstract

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.

Keywords: Binding affinity; Bovine serum albumin; Curcumin; Protein modification; Pulsed electric field.

MeSH terms

Curcumin*
Electricity
Hydrophobic and Hydrophilic Interactions
Protein Binding
Serum Albumin, Bovine* / metabolism
Spectrometry, Fluorescence

Substances

Serum Albumin, Bovine
Curcumin