Ying Ma
Harbin Institute of Technology, China
Title: Binding characteristics of curcumin to β-Lactoglobulin
Biography
Biography: Ying Ma
Abstract
Curcumin (CCM) is a phenolic compound and has been shown to exhibit many bioactivities, but it is extremely limited in its application due to its insolubility in water. β-Lactoglobulin (β-Lg) is a major whey protein and has an ability to bind hydrophobic molecules because of its hydrophobic core. In this experiments, the binding of CCM to β-Lg was investigated. The results showed that binding CCM to β-Lg leads to a partial change in protein structure. CCM was bound respectively to two different sites of protein at pH 6.0 and pH 7.0 via hydrophobic interaction. CCM-β-Lg complex was formed by one molecule of protein combining with one molecule of CCM. The solubility of CCM was increased by 15954-fold through the complex. The β-Lg -CCM complex and CCM in complex had a good stability in the pH range of 2 to 8. The results of antioxidant experiments showed that the ABTS and hydroxyl radical scavenging capacity of CCM was reduced by binding with β- Lg, but the total reducing ability of CCM was improved.