Journal
LWT-FOOD SCIENCE AND TECHNOLOGY
Volume 173, Issue -, Pages -Publisher
ELSEVIER
DOI: 10.1016/j.lwt.2022.114352
Keywords
Oleosome protein; Self -assembly; Nanoparticles; Curcumin
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Guanidine hydrochloride (GuHCl) was employed to disassemble and reassemble oleosome proteins (OP), leading to the encapsulation of curcumin inside OP core-shell structures, improving its stability and bioavailability. The disassembly and reassembly of OP were primarily attributed to the breakage and formation of hydrogen bonds. Curcumin bound preferentially with extrinsic protein of OP to form protein-nanoparticle shells via hydrogen bonding and hydrophobic interactions, while intrinsic-protein formed hydrophobic cores that encapsulated curcumin. The final encapsulation efficiency of curcumin was 22.56 µmol/mg. Moreover, the curcumin-OP nanoparticles exhibited high stability and bioavailability (44.7%) with sustained-release behavior using GuHCl (5 M).
Guanidine hydrochloride (GuHCl) was used to disassemble and reassemble oleosome proteins (OP) to encap-sulate curcumin inside OP core-shell structures, improving its stability and bioavailability. The effect of GuHCl on the structure of OP indicated that OP disassembly and reassembly primarily involved the breakage and formation of hydrogen bonds. The extrinsic-protein subunits in OP were completely disassembled by GuHCl (5 M); after GuHCl removal by dialysis, the disassembled subunits were re-linked with intrinsic-protein subunits, encapsulating curcumin during the reassembly process. Curcumin preferentially bound with extrinsic protein of OP (through hydrogen bonding and hydrophobic interactions) to form protein-nanoparticle shells, while intrinsic-protein formed hydrophobic cores that encapsulated curcumin; the final curcumin encapsulation effi-ciency was 22.56 mu m/mg. Additionally, the curcumin-OP nanoparticles exhibited high stability and bioavail-ability (44.7%), and sustained-release behavior with GuHCl (5 M). This study elucidates and develops OP structures and could guide the development of high-efficiency nanoparticle delivery systems for hydrophobic nutrient carriers.
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