%0 Journal Article
%T Goose liver protein emulsion with enhanced interfacial stabilization by facile core-shell curcumin complexation.
%A Hu Y
%A Sun Y
%A Zhou C
%A Zeng X
%A Du L
%A Xia Q
%A Pan D
%A Wang W
%J Int J Biol Macromol
%V 274
%N 0
%D 2024 Aug 20
%M 38908636
%F 8.025
%R 10.1016/j.ijbiomac.2024.133324
%X The role of facile curcumin dispersion and its hydrophobic complexation onto GLP, in the form of shell (GLPC-E), core (GLPE-C) and with synergy (GLP-ECE), on the protein interfacial and emulsion stabilization was investigated. Turbiscan instability index, microrheological elasticity, viscosity and solid-liquid balance values showed that the O/W emulsion stability was in the order of GLP-E < GLPC-E < GLPE-C < GLP-ECE. GLP-ECE also gave the most reduced D [4, 3] (8.11 ± 0.14 μm) with lowest indexes of flocculation (2.80 ± 0.05 %) and coalescence (2.83 ± 0.10 %) at day 5. Interfacial shear rheology suggested the GLP-curcumin complexation fortified the GLP interfacial gelling and then the efficiency as steric stabilizer, especially of core-shell complexation (14.2 mN/m) that showed the most sufficient in-plane protein interaction against strain. Dilatational elasticity and desorption observation revealed the synergistic curcumin complexation facilitated GLP unfolding and macromolecular association at O/W interface, as was also verified from SEM image and surface hydrophobicity (from 36.23 to 76.04). Overall, this study firstly reported the facile curcumin bi-physic dispersion and GLP complexation in improving the emulsion stabilizing efficiency of the protein by advancing its interfacial stabilization.