盐离子和pH对去amid化大豆蛋白质水凝形成的影响:分子结构,热聚合和网络
Tang-Hao Li1, Yao-Qin Yang1, Gao-Shang Wang1
1Laboratory of Food Proteins and Colloids, School of Food Science and Engineering, Guangdong Province Key Laboratory for Green Processing of Natural Products and Product Safety, South China University of Technology, Guangzhou 510640, PR China.
Food chemistry
|December 21, 2024
概括
诸如盐离子和pH等环境因素显著影响脱amid化大豆蛋白分离物 (DSPI) 热凝. 较高的盐度和酸性pH值提高了DSPI凝网络的强度和粘性弹性.
科学领域:
- 食品科学 食品科学 食品科学
- 蛋白质化学 蛋白质化学
- 材料科学 材料科学 材料科学
背景情况:
- 脱氧化大豆蛋白分离物 (DSPI) 是一种有价值的食品成分.
- 了解其热凝对于食品加工至关重要.
- 环境因素会影响蛋白质的结构和功能.
研究的目的:
- 为了研究盐离子 (Ca2+,Mg2+,Na+) 和pH对DSPI热凝的影响.
- 阐明环境条件,分子结构和凝特性之间的关系.
主要方法:
- 在不同盐离子度和pH值下对DSPI进行热凝试验.
- 风湿学测量以评估粘性弹性和凝强度.
- 结构分析观察蛋白质聚合和网络形成.
主要成果:
- 盐离子度的增加导致了更大的DSPI聚合物和增强的凝粘性.
- 通过离子增强强度的顺序是Ca2+ > Mg2+ > Na+.
- 将pH值从11调到3导致DSPI中的结构排序,促进聚合并加强凝网络.
结论:
- 环境因素,特别是盐离子和pH值,在调节DSPI热凝方面发挥着至关重要的作用.
- DSPI的分子结构和聚合行为是环境对凝性质影响的关键媒介.
- 这项研究为优化食品工业中DSPI应用提供了基础知识.
更多相关视频
08:50Easy Manipulation of Architectures in Protein-based Hydrogels for Cell Culture Applications
Published on: August 4, 2017
6.7K
15:33Microwave-assisted Functionalization of Polyethylene glycol and On-resin Peptides for Use in Chain Polymerizations and Hydrogel Formation
Published on: October 29, 2013
28.8K
相关概念视频
Protein Denaturation
3.9K
The function of proteins depends on their native three-dimensional structure, which is dictated by the amino acid sequence of the specific protein. Folding of the polypeptide chain takes place under specific conditions that energetically favor the folded conformation. In contrast, protein denaturation occurs spontaneously under unfavorable conditions that disrupt the integrity of the folded conformation. Thus, the chemical and physical environment of a protein, such as significant changes in pH...
3.9K
SDS-PAGE
27.3K
Gel electrophoresis is a method that separates biological macromolecules like nucleic acids or proteins by forcing them to pass through a gel matrix under an electric field.
A variation of gel electrophoresis, termed polyacrylamide gel electrophoresis (PAGE), is commonly used for separating proteins according to their molecular size by passing them through a polyacrylamide gel. Because of the varying charges associated with amino acid side chains, PAGE can be used to separate intact...
A variation of gel electrophoresis, termed polyacrylamide gel electrophoresis (PAGE), is commonly used for separating proteins according to their molecular size by passing them through a polyacrylamide gel. Because of the varying charges associated with amino acid side chains, PAGE can be used to separate intact...
27.3K
Protein Folding
117.3K
Overview
117.3K
