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

Kunyu Ren; Xinru Cao; Lexi Zheng; Shi Liu; Lanxin Li; Lin Cheng; Tian Tian; Xiaohong Tong; Huan Wang; Lianzhou Jiang

doi:10.1016/j.ijbiomac.2024.131900

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

Int J Biol Macromol. 2024 Apr 26;269(Pt 1):131900. doi: 10.1016/j.ijbiomac.2024.131900. Online ahead of print.

Authors

Kunyu Ren¹, Xinru Cao¹, Lexi Zheng¹, Shi Liu¹, Lanxin Li¹, Lin Cheng¹, Tian Tian², Xiaohong Tong³, Huan Wang⁴, Lianzhou Jiang¹

Affiliations

¹ College of Food Science, Northeast Agricultural University, Harbin, Heilongjiang 150030, China.
² College of Food Science and Engineering, Hainan University, Haikou, Hainan 570228, China.
³ College of Agricultural, Northeast Agricultural University, Harbin, Heilongjiang 150030, China. Electronic address: tongxiaohong0110@163.com.
⁴ College of Food Science, Northeast Agricultural University, Harbin, Heilongjiang 150030, China. Electronic address: whname@neau.edu.cn.

PMID: 38677675
DOI: 10.1016/j.ijbiomac.2024.131900

Abstract

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.

Keywords: Digestion; Liposome; Soy protein.