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Updated: Jul 5, 2025
Solubility of Hydrophobic Compounds in Aqueous Solution Using Combinations of Self-assembling Peptide and Amino Acid
Published on: September 20, 2017
Self-assembly embedding of curcumin by alkylated rice bran protein
Ning Wang1, Weining Wang1, Hairong Zhang2
1College of Food Engineering, Key Laboratory of Food Science and Engineering of Heilongjiang Ordinary Higher Colleges, Key Laboratory of Grain Food and Comprehensive Processing of Heilongjiang Province, Harbin University of Commerce, Harbin 150028, China.
Abstract:
Lysine-rich rice bran protein (RBP) can be used as raw material for alkylation modification to improve the self-assembly performance of protein. The results of 1H NMR, degree of alkylation, and DSC analysis showed that the alkyl chain was successfully attached to the RBP. The surface hydrophobicity and absolute ζ-potential increased. The three-dimensional structure of the alkylated RBP (ARBP) become more porous and ARBP-2 was selected as the material for embedding curcumin. The XRD results revealed that curcumin induced self-aggregation of ARBP-2 and the inclusion of curcumin was attained. The maximum encapsulation efficiency of curcumin was 82.67 % and the maximum loading amount was 171.37 g/100 g RBP. The results of atomic force microscopy (AFM), particle size, and polydispersity index (PDI) analyses revealed that the particles in the system were aggregated after curcumin was added. Curcumin was well protected by encapsulation in the self-assembled particles. Thus, this study provides a new strategy for the embedding and delivery of curcumin.
