从分子相互作用到宏观稳定性:通过多尺度动力学揭示的结构性可塑性,离子强度如何调节鱼类肌纤维蛋白吸附
Yueqi Wang1, Yamei Wu2, Huan Xiang1
1Key Laboratory of Aquatic Product Processing, Ministry of Agriculture and Rural Affairs, National R&D Center for Aquatic Product Processing, South China Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Guangzhou 510300, China.
Food chemistry
|August 15, 2025
概括
肌纤维蛋白 (MPs) 在油/水接口的吸附是乳液稳定性的关键. 在0.6mol/L的离子强度下达到最佳稳定性,增强了界面膜弹性和抗变形性.
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
- 体科学 体科学 体科学
背景情况:
- 肌纤维蛋白 (MP) 在食品系统中至关重要,特别是在乳液中.
- 了解它们的界面行为对于控制乳液稳定性至关重要.
- 离子强度显著影响蛋白质-蛋白质和蛋白质接口相互作用.
研究的目的:
- 使用多尺度方法研究MP的接口吸附.
- 阐明MPs在不同离子强度下稳定乳液的分子机制.
- 为了确定MP稳定乳液的最佳离子强度.
主要方法:
- 接口吸附的多尺度分析.
- 测量蛋白质结构变化和在界面上的方向.
- 对面膜特性 (厚度,质量,弹性) 的评估.
- 评估乳液稳定性和抗变形能力.
主要成果:
- MP吸附受静电和疏水相互作用的控制.
- 高离子强度 (0.6-1.0mol/L) 增加了MP扩散系数 (Kdiff).
- 介面膜厚度和质量与离子强度有显著的变化.
- 表面膜弹性和最佳乳液稳定性的峰值发生在0.6mol/L的离子强度.
结论:
- 离子强度严重影响MP界面行为和乳液稳定性.
- 这项研究提供了在油/水接口上对MP吸附的分子理解.
- 结果为在食品乳液中应用MP提供了理论和方法指导.
- 确定了基于MP的乳液稳定最佳条件.
相关概念视频
Cell-matrix's Response to Mechanical Forces
2.7K
In animal cells, the extracellular matrix allows cells within tissues to withstand external stresses and transmits signals from the outside of the cell to the inside. The extracellular matrix is extensive, and its composition varies between different types of tissues. For example, the reticular fibers and ground substance make up the ECM in loose connective tissue, while collagen and bone minerals make up the ECM of bone tissue.
Anchoring junctions mechanically attach a cell to the...
Anchoring junctions mechanically attach a cell to the...
2.7K
Adaptability of Cytoskeletal Filaments
3.9K
The cytoskeleton is a complex dynamic structure performing varied functions based on cellular requirements. The adaptability of the individual filaments in the cytoskeleton determines their ability to perform various functions within the cell. It can undergo rapid reorganization during processes like cell division or remain stable for several hours as in the interphase. The adaptability of these filaments depends on stringent regulatory mechanisms. The microfilament and microtubules of the...
3.9K
Actin and Myosin in Muscle Contraction
14.7K
Actin and myosin are contractile proteins that form the sarcomere found in skeletal muscle tissues for regulating muscle contraction. Actin, a globular contractile protein, interacts with myosin for muscle contraction. The skeletal tissue appears striped or striated under a microscope due to the repeated arrangement of contractile proteins actin and myosin along the length of myofibrils. Dark A bands and light I bands repeat along myofibrils, and the alignment of myofibrils in the cell causes...
14.7K
Smooth Muscle Contraction
3.9K
Smooth muscle contraction is a complex process vital for various bodily functions, from maintaining blood vessel tension to facilitating the movement of food through the digestive tract. Unlike striated muscles, smooth muscle contraction begins more slowly and lasts longer.
The onset of contraction is triggered by an increase in calcium ions within the sarcoplasm, similar to the process in striated muscle. However, smooth muscles have a relatively smaller reservoir of the sarcoplasmic...
The onset of contraction is triggered by an increase in calcium ions within the sarcoplasm, similar to the process in striated muscle. However, smooth muscles have a relatively smaller reservoir of the sarcoplasmic...
3.9K
Studying the Cytoskeleton
6.9K
The cytoskeletal architecture can be studied using different microscopic and biochemical techniques. Electron microscopy was instrumental in discovering the cytoskeletal architecture around the 1960s, which allowed obtaining structural information at a high-resolution level. However, the sample preparation procedure often limits this ability in biological samples. Several protocols have been developed over the years to optimize sample preparation. In one of the protocols known as rotary...
6.9K
The Sarcomere
9.3K
A sarcomere is a microscopic segment repeating in a myofibril. The sarcomere fundamentally consists of two main myofilaments: thick filaments called myosin and thin filaments called actin. These filaments interact by sliding past each other in response to stimulus. In addition to myosin and actin, several other proteins, such as tropomyosin, troponin, titin, nebulin, myomesin, α-actinin, and dystrophin, play crucial roles in regulating, structuring, and functioning of the sarcomere.
Each...
Each...
9.3K


