High internal phase emulsion stabilized by soy protein isolate-Rutin complex: Rheological properties, bioaccessibility and in vitro release kinetics.

Autor: Zhao J; College of Tourism and Cuisine, Harbin University of Commerce, Harbin, Heilongjiang 150028, China; Postdoctoral Programme of Meteria Medical Institute, Harbin University of Commerce, Harbin 150028, China. Electronic address: zhaojuyang1987@hotmail.com., Chen Y; Postdoctoral Programme of Meteria Medical Institute, Harbin University of Commerce, Harbin 150028, China., Xu S; Postdoctoral Programme of Meteria Medical Institute, Harbin University of Commerce, Harbin 150028, China., Fang X; Postdoctoral Programme of Meteria Medical Institute, Harbin University of Commerce, Harbin 150028, China., Yang F; Postdoctoral Programme of Meteria Medical Institute, Harbin University of Commerce, Harbin 150028, China., Li Y; Academy of Agricultural Planning and Engineering, Ministry of Agriculture and Rural Affairs, Beijing 100125, China. Electronic address: liyuanyuan.1992@163.com.
Jazyk: angličtina
Zdroj: International journal of biological macromolecules [Int J Biol Macromol] 2024 Nov; Vol. 280 (Pt 2), pp. 135748. Date of Electronic Publication: 2024 Sep 19.
DOI: 10.1016/j.ijbiomac.2024.135748
Abstrakt: High internal phase emulsions (HIPEs) are promising carrier materials for encapsulating and delivering hydrophobic bioactive compounds. By strategically adjusting the composition, particle size, or charge of HIPEs, it is possible to enhance both their stability and the bioaccessibility of hydrophobic polyphenols encapsulated within them. In this study, different soy protein isolate (SPI)-rutin (SPI-R) complexes (formed under various preheating temperatures) were used to stabilize HIPEs, while the particle size, and charge of HIPEs was further adjusted through different homogenization rates. The results demonstrated that an optimal preheating temperature of 70 °C for the complex and a homogenization rate of 15,000 rpm for HIPEs enhanced the stability of the entire emulsion system by producing more uniform and smaller droplet distribution with improved rheological properties. Furthermore, in vitro digestion experiments showed that HIPEs stabilized by the SPI-R complexes (HSR) at optimal homogenization rate had better loading efficiency (98.68 %) and bioaccessibility compared to other groups. Additionally, fitting results from release kinetics confirmed that rutin encapsulated by HSR could achieve sustained release effect. Overall, these findings suggest that HSR has great potential as an effective vehicle for delivering hydrophobic bioactive compounds like rutin within the food industry.
Competing Interests: Declaration of competing interest Juyang Zhao reports financial support was provided by Heilongjiang Provincial Postdoctoral Science Foundation (LBH-Z2204). Juyang Zhao reports financial support was provided by 2023 Harbin University of Commerce Teacher “Innovation” Project (2023-KYYWF-0992). If there are other authors, they declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
(Copyright © 2024. Published by Elsevier B.V.)
Databáze: MEDLINE
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