相关实验视频

Updated: Sep 20, 2025

Extraction of Plant-based Capsules for Microencapsulation Applications

Extraction of Plant-based Capsules for Microencapsulation Applications

Published on: November 9, 2016

洞察hesperidin的功能化:被大豆蛋白分离物和多糖化合物复合体封装

Weiben Ge¹, Jinghui Chen¹, Yv Wang¹

¹School of Food Science & Technology, Jiangnan University, Wuxi, Jiangsu, 214122, PR China.

|May 28, 2025

概括

大豆蛋白质分离物与香甘结合,有效封装hesperidin,增强其稳定性和生物可访问性. 这种蛋白质-多糖化合物复合体显示出对食品成分应用的前景.

科学领域:

食品科学与技术食品科学与技术
生物材料科学生物材料科学
营养生物化学营养生物化学

背景情况:

蛋白质多糖化合物复合物为活性成分封装提供独特的特性.
大豆蛋白质分离物 (SPI) 和各种多糖化合物 (基托,瓜尔,桑坦) 正在探索它们的封装潜力.

研究的目的:

为了研究使用SPI与不同多糖化合物相结合的hesperidin (HP) 的封装.
评估封装 hesperidin 的物理化学性质,稳定性和生物活性.

主要方法:

复杂化SPI与奇托,瓜尔和桑坦 (XG) 封装hesperidin.
评估封装效率,颗粒大小,储存稳定性,发泡和乳化特性.
谱分析和分子对接以阐明相互作用机制.
评估α-葡萄糖酶抑制和hesperidin的生物可访问性.

主要成果:

该SPI/XG复合体实现了最高的封装效率 (90.22%) 和卓越的存储稳定性.
复杂的形成涉及结合,疏水性和离子静电相互作用.
增加的XG含量增强了泡和乳化稳定性.
三元复合体显示出显著的α-葡萄糖酶抑制和改善HP生物可访问性.

结论:

赞坦是一种有效的材料,可以将hesperidin与大豆蛋白质分离物封装在一起.
开发的SPI-XG复合物增强了hesperidin的稳定性,生物可访问性和功能性质.
这种方法为将活性成分纳入食品中提供了一种新的策略.

关键词:

复杂的复杂的复杂.功能性质功能性质功能性质赫斯佩里迪因是人类的一种药物.离子/非离子多糖类这是一种大豆蛋白质分离物.

更多相关视频

Preparation and Characterization of Nanoliposomes for the Entrapment of Bioactive Hydrophilic Globular Proteins

Preparation and Characterization of Nanoliposomes for the Entrapment of Bioactive Hydrophilic Globular Proteins

Published on: August 31, 2019

Synthesis of an Intein-mediated Artificial Protein Hydrogel

Synthesis of an Intein-mediated Artificial Protein Hydrogel

Published on: January 27, 2014

相关概念视频

Protein Complexes with Interchangeable Parts

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...

Oligosaccharide Assembly

Oligosaccharide Assembly

Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...

Protein Complex Assembly

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types. Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...