从surimi废水中冷等离子沉的sarcoplasmic蛋白质:二相蛋白质的差异性结构修饰介导动态转换
Qiang Li1, Jianfeng Lu1, Zhicheng Cai1
1Engineering Research Center of Bio-process, MOE, School of Food and Biological Engineering, Hefei University of Technology, Hefei, China; Anhui Province Key Laboratory for Agriculture Products Modern Processing, School of Food and Biological Engineering, Hefei University of Technology, Hefei, China.
Food chemistry
|January 31, 2026
概括
冷等离子体 (CP) 处理选择性地从surimi废水中沉了sarcoplasmic蛋白质 (SP). CP破坏蛋白质结构,通过形状变化和交叉链接促进聚合和沉.
科学领域:
- 生物化学 生物化学
- 食品科学 食品科学 食品科学
- 血技术是一项技术.
背景情况:
- 苏里米的废水含有有价值的肉质蛋白质 (SP),需要有效的回收.
- 冷等离子体 (CP) 是一种新兴技术,在食品加工和废水处理方面具有潜在的应用.
研究的目的:
- 在surimi废水中研究由冷等离子体 (CP) 诱导的肉质等离子体蛋白 (SP) 沉的机制.
- 为了阐明在CP处理过程中SP的结构和化学变化.
主要方法:
- 苏里米废水用冷等离子体处理.
- 分析总和未沉积的SP.分析.
- 测量内在光和二次结构 (β-片).
- 评估和二硫化物键的含量.
- 凝电泳和分子对接.
主要成果:
- CP治疗导致SP的部分沉,导致两相分布.
- CP破坏了SP的高阶结构,增加了β片含量和内在光.
- 形成可溶性聚合物,通过和二硫化物键相互连接,导致沉物形成.
- 离子电点附近的CP处理溶液的酸化加剧了形状和共价变化.
- 对SP分子对反应性物种的差异反应确定了选择性降水.
结论:
- 冷等离子体通过结构破坏和交叉链接诱导了sarcoplasmic蛋白质的选择性沉.
- 该机制涉及最初的结构变化,其次是聚合和沉,受pH值和蛋白质特异反应性的影响.
- 了解这些机制可以优化使用CP技术从surimi废水中优化SP回收.
相关概念视频
Protein and Protein Structure
87.6K
Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...
A protein's shape is critical to its function. For example, an enzyme...
87.6K
Structural Protein Function
29.9K
Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity. In bones and teeth, it mineralizes to...
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity. In bones and teeth, it mineralizes to...
29.9K
Structural Protein Function
3.3K
3.3K
Protein and Protein Structures
19.1K
19.1K
Protein Modifications in the RER
7.1K
Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
7.1K
Protein Kinases and Phosphatases
15.1K
Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
15.1K


