AI Article Synopsis
- Lysine-rich rice bran protein (RBP) underwent alkylation modification to enhance its self-assembly properties, with successful attachment of alkyl chains confirmed through various analyses.
- The modified protein, referred to as ARBP-2, exhibited increased hydrophobicity and a more porous structure, making it suitable for embedding curcumin.
- Curcumin had an encapsulation efficiency of 82.67% within the ARBP-2 matrix, demonstrating that the self-assembled particles effectively protected curcumin during the process.
Article 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 H 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.
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| http://dx.doi.org/10.1016/j.ijbiomac.2024.129627 | DOI Listing |
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