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Updated: May 10, 2026

Solubility of Hydrophobic Compounds in Aqueous Solution Using Combinations of Self-assembling Peptide and Amino Acid
Published on: September 20, 2017
Curcumin loading in Camellia seed oil body and multi-compartment emulsion fabrication: effect of high-pressure
Fangyuan Chen1, Muwen Lu1, Michael A Rogers2
1Guangdong Provincial Key Laboratory of Nutraceuticals and Functional Foods, College of Food Science, South China Agricultural University, Guangzhou 510640, People's Republic of China.
Abstract:
In this study, multi-compartment emulsion based on camellia seed oil bodies (CSO) were engineered for co-encapsulation of lipophilic bioactive compounds. High-pressure homogenization (HPH) was employed to modulate CSO size distribution and interfacial properties (surface hydrophobicity and protein conformation) of CSO. Results demonstrated that HPH treatment at 90 MPa dramatically reduced CSO-90 diameter from 1498.00 nm to 280.87 nm. This processing concurrently induced CSO interface protein unfolding, leading to significant increase in surface hydrophobicity and remarkable enhancement in curcumin (Cur) loading capacity. This size-tunable HPH processed CSO particles was complexed with chitosan (CS) and further used to stabilize high internal phase emulsions (HIPEs). The smaller CSO-90-CS particles was particular effective in stabilizing HIPEs co-encapsulating Cur and algal oil. This was probably facilitated by robust viscoelastic interfacial film formation. The resultant HIPEs exhibited enhanced functional properties, including increased gel strength, free radical scavenging capacity and oxidative stability (peroxide value reduced to 55 % of control; TBARS concentration maintained below 1.80 μg MDA/g algal oil during 8 days storage at 50 °C). This interfacial engineering strategy provides a promising platform for co-delivery and stabilization of oxidation-sensitive bioactive compounds, contributing to development of clean-label and nutrient-dense functional food products with enhanced physicochemical and bioactive stability.

