4.7 Article

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

期刊

FOOD CHEMISTRY
卷 377, 期 -, 页码 -

出版社

ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2021.131945

关键词

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

资金

  1. National Natural Science Foundation of China [32172348]
  2. S&T projects of Guangdong Province [2019B020212004]
  3. S&T Project of Guangzhou [202102080346]
  4. 111 Project [B17018]

向作者/读者索取更多资源

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.
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.

作者

我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。

评论

主要评分

4.7
评分不足

次要评分

新颖性
-
重要性
-
科学严谨性
-
评价这篇论文

推荐

暂无数据
暂无数据