用于β-胡卜素输送的粉样纤维 - - 自组装结构对结合和体外释放行为的影响
Congying Chen1, Haifeng Wang1, Qing Wang1
1School of Food Science and Biotechnology, Zhejiang Gongshang University, Hangzhou 310018, China.
Food chemistry
|November 7, 2024
概括
产生了具有不同结构的乳清蛋白分离粉样蛋白纤维素 (WPIF). 类似虫的WPIF更好地封装了β-胡卜素 (BC),但在消化过程中与延长的WPIF相比,它在消化过程中释放得更快.
科学领域:
- 食品科学 食品科学 食品科学
- 生物材料科学 生物材料科学
- 营养科学 营养科学
背景情况:
- 乳清蛋白分离物 (WPI) 可以自组装成粉样蛋白纤维 (WPIF).
- WPIF的结构可以影响其属性,例如表面疏水性和结合能力.
- β-胡卜素 (BC) 是一种具有较低生物可用性的重要营养素.
研究的目的:
- 研究WPIF结构对β-胡卜素 (BC) 结合和体外可消化的影响.
- 为了比较不同的WPIF结构中的BC的封装效率和释放动力学.
主要方法:
- 准备两个不同的WPIF结构:延长型 (E-WPIF) 和类似虫的 (W-WPIF).
- 描述WPIF表面的疏水性.
- 在WPIF内评估BC封装效率和负载能力.
- 在体外胃肠道消化模型评估BC释放.
主要成果:
- 与E-WPIF相比,W-WPIF表现出更高的表面疏水性和更高的BC封装效率和负载能力.
- 鉴定出疏水相互作用是WPIF/BC结合的主要作用力.
- 在消化过程中,WPIF结构降解,释放BC. 由于结合较弱和消化能力更好,E-WPIF/BC的BC释放率高于W-WPIF/BC.
结论:
- WPIF结构显著影响消化过程中的BC结合和释放.
- W-WPIF提供了增强的BC封装,但E-WPIF促进了更快的BC释放,根据所需的释放配置文件提出了潜在的应用.
相关概念视频
Amyloid Fibrils
9.3K
Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...
9.3K
Protein Folding
117.4K
Overview
117.4K


