弗洛雷丁对乳制品蛋白模型中阿克罗林诱导的蛋白质修饰和物理化学变化的影响
Yanming Zhang1, Xingya Hao2, Zhangjie Hu2
1Jiaxing Key Laboratory for Research and Application of Green and Low-carbon Advanced Materials, School of Advanced Materials Engineering, Jiaxing Nanhu University, Jiaxing 314001, PR China.
Food chemistry: X
|December 9, 2024
概括
氨酸 (Phl) 有效地保护乳清蛋白分离物 (WPI) 免受由氨酸 (ACR) 引起的损伤. 清除了ACR,防止了蛋白质的修饰,并保存了蛋白质的结构和功能.
科学领域:
- 食品化学 食品化学
- 蛋白质化学 蛋白质化学
- 生物化学 生物化学
背景情况:
- 氨酸 (ACR) 是一种反应性α,β不和化物,已知可以修改蛋白质.
- 饮食中的蛋白质可能会经历不良的修改,影响其营养和功能性质.
研究的目的:
- 研究一种类化合物 - - 佛洛 (Phl) 的保护作用,以防止乳清蛋白分离物 (WPI) 发生由阿克罗莱因引起的变化.
- 评估Phl减轻对蛋白质的烯蛋白损伤的机制.
主要方法:
- 乳清蛋白分离物 (WPI) 在有或没有洛 (Phl) 的情况下用阿克罗莱因 (ACR) 治疗.
- 测量了蛋白质碳烯酸含量,总硫含量,表面水性和内在光.
- 西方斑点分析被用于可视化ACR纳入WPI.
- 评估了Phl-ACR引证的形成.
主要成果:
- (2毫米) 显著降低了ACR诱导的蛋白质碳基 (从1.65到0.65微摩尔/毫克蛋白质) 和保存的硫含量 (从0.28到0.24微摩尔/毫克蛋白质).
- Phl降低了蛋白质表面的疏水性和内在的光.
- 西方布洛特证实Phl公司中断了ACR加入WPI的过程.
- 只有2.87%的ACR仍然存在,有Phl-ACR引证形成的证据.
结论:
- Phl有效地清除ACR,从而保护WPI免受阿克罗莱因诱导的损伤.
- 通过防止ACR修饰,Phl减轻了对蛋白质结构和功能的不良影响.
- 像Phl这样的天然化合物显示出保护食蛋白质免受反应性化物影响的潜力.
相关概念视频
Covalently Linked Protein Regulators
6.8K
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
These groups modify specific amino acids in a protein....
6.8K
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
Protein Modifications in the RER
5.0K
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...
5.0K


