The interaction between bovine serum albumin and [6]-,[8]- and [10]-gingerol: An effective strategy to improve the solubility and stability of gingerol

作者：Zhong, Li; Wang, Rui; Wen, Qin-Hui; Li, Jian; Lin, Jia-Wei; Zeng, Xin-An^*

来源：Food Chemistry, 2022, 372: 131280.

DOI：10.1016/j.foodchem.2021.131280

• Gingerols
• Bovine serum albumins
• Fluorescence
• Molecular modelling
• Binding interaction

In this study, the binding mechanism between bovine serum albumin (BSA) and three gingerols ([6]-, [8]- and [10]-gingerol) was evaluated to explore an effective strategy for improving solubility and stability of gingerols. The fluorescence analysis suggested gingerols could bind with BSA to form a stable BSA/gingerols complex and [10]-gingerol had the strongest binding affinity (Ka = 4.016 x 104 L/mol) at 298 K. Thermodynamic parameters and molecular modeling validated that hydrophobic interaction and hydrogen bonds were the main driving force for the interaction of BSA/gingerols. Gingerols bound to BSA at site I (subdomain IIA) resulted in a conformational change of BSA with a structure shrinkage, which was responsible for the decrease of surface hydrophobicity. The formation of BSA/gingerols complexes promoted the solubility of [6]-, [8]- and [10]-gingerol increasing by 1.50, 6.04 and 23.50 times, respectively. In addition, the stability and antioxidant capacity of gingerols was significantly improved after binding with BSA.