Liposomes decorated with β-conglycinin and glycinin: Construction, structure and in vitro digestive stability.

Autor: Ren K; College of Food Science, Northeast Agricultural University, Harbin, Heilongjiang 150030, China., Cao X; College of Food Science, Northeast Agricultural University, Harbin, Heilongjiang 150030, China., Zheng L; College of Food Science, Northeast Agricultural University, Harbin, Heilongjiang 150030, China., Liu S; College of Food Science, Northeast Agricultural University, Harbin, Heilongjiang 150030, China., Li L; College of Food Science, Northeast Agricultural University, Harbin, Heilongjiang 150030, China., Cheng L; College of Food Science, Northeast Agricultural University, Harbin, Heilongjiang 150030, China., Tian T; College of Food Science and Engineering, Hainan University, Haikou, Hainan 570228, China., Tong X; College of Agricultural, Northeast Agricultural University, Harbin, Heilongjiang 150030, China. Electronic address: tongxiaohong0110@163.com., Wang H; College of Food Science, Northeast Agricultural University, Harbin, Heilongjiang 150030, China. Electronic address: whname@neau.edu.cn., Jiang L; College of Food Science, Northeast Agricultural University, Harbin, Heilongjiang 150030, China.
Jazyk: angličtina
Zdroj: International journal of biological macromolecules [Int J Biol Macromol] 2024 Jun; Vol. 269 (Pt 1), pp. 131900. Date of Electronic Publication: 2024 Apr 26.
DOI: 10.1016/j.ijbiomac.2024.131900
Abstrakt: Liposomes were modified with different proportions of β-conglycinin (7S) and glycinin (11S) to form Lip-7S and Lip-11S. The morphology, interaction and in vitro simulated digestion of liposomes were studied. The particle size of Lip-7S was smaller than that of Lip-11S. When the values of Lip-7S and Lip-11S were 1:1 and 1:0.75, respectively, the ζ-potential had the maximum absolute value and the dispersion of the system was good. The results of multispectral analysis showed that hydrogen-bond and hydrophobic interaction dominated protein-modified liposomes, the protein structure adsorbed on the surface of liposomes changed, the content of α-helix decreased, and the structure of protein-modified liposomes became denser. The surface hydrophobicity and micropolarity of liposomes decreased with the increase of protein ratio, and tended to be stable after Lip-7S (1:1) and Lip-11S (1:0.75). Differential scanning calorimetry showed that Lip-7S had higher phase transition temperature (≥170.5 °C) and better rigid structure. During simulated digestion, Lip-7S (22.5 %) released less Morin than Lip (40.6 %) and Lip-11S (26.2 %), and effectively delayed the release of FFAs. The environmental stability of liposomes was effectively improved by protein modification, and 7S had better modification effect than 11S. This provides a theoretical basis for 7S and 11S modified liposomes, and also provides a data reference for searching for new materials for stabilization of liposomes.
Competing Interests: Declaration of competing interest We confirm that none of the data and research in the draft was made public or published. There are no conflicts of interest.
(Copyright © 2024 Elsevier B.V. All rights reserved.)
Databáze: MEDLINE
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