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From molecular interactions to macroscopic stability: How ionic strength modulates fish myofibrillar protein adsorption via structural plasticity as revealed by multiscale dynamics.

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Názov: From molecular interactions to macroscopic stability: How ionic strength modulates fish myofibrillar protein adsorption via structural plasticity as revealed by multiscale dynamics.
Autori: Wang Y; Key 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., Wu Y; Key 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; College of Food Science and Engineering, Ocean University of China, Qingdao 266000, China., Xiang H; Key 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., Sun-Waterhouse D; Key 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; School of Chemical Sciences, The University of Auckland, Private Bag, 92019, Auckland, New Zealand., Chen S; Key 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., Zhao Y; Key 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., Wu Y; Key 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. Electronic address: wuyygd@163.com., Waterhouse GIN; School of Chemical Sciences, The University of Auckland, Private Bag, 92019, Auckland, New Zealand. Electronic address: g.waterhouse@auckland.ac.nz.
Zdroj: Food chemistry [Food Chem] 2025 Nov 30; Vol. 493 (Pt 3), pp. 145819. Date of Electronic Publication: 2025 Aug 06.
Spôsob vydávania: Journal Article
Jazyk: English
Informácie o časopise: Publisher: Elsevier Applied Science Publishers Country of Publication: England NLM ID: 7702639 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1873-7072 (Electronic) Linking ISSN: 03088146 NLM ISO Abbreviation: Food Chem Subsets: MEDLINE
Imprint Name(s): Publication: Barking : Elsevier Applied Science Publishers
Original Publication: Barking, Eng., Applied Science Publishers.
Výrazy zo slovníka MeSH: Fish Proteins*/chemistry , Muscle Proteins*/chemistry , Myofibrils*/chemistry, Adsorption ; Osmolar Concentration ; Animals ; Emulsions/chemistry ; Hydrophobic and Hydrophilic Interactions ; Fishes
Abstrakt: Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
This study employed a multi-scale approach to elucidate the interfacial adsorption behavior of myofibrillar proteins (MPs) and the molecular mechanisms underlying emulsion stability under different ionic strengths. The interfacial adsorption of MPs primarily depends on electrostatic and hydrophobic interactions. When MPs approach the interface, structural changes occur, accompanied by angular deflection and orientation towards the horizontal direction. High ionic strengths (0.6-1.0 mol/L) enhance the K diff of MPs, with the thickness and mass of the interface film showing significant changes as ionic strength increases (1 > 0.8 > 0.4 > 0.6 > 0.2 > 0). At 0.6 mol/L, the elasticity of the interface film reaches its peak, the emulsion exhibits the strongest deformation resistance, and achieves optimal stability. This discovery deepens our understanding of protein adsorption behavior at oil/water interfaces and provides new theoretical basis and methodological guidance for the practical application of MPs in the field of food emulsions.
(Copyright © 2024. Published by Elsevier Ltd.)
Contributed Indexing: Keywords: Interfacial adsorption behavior; Molecular dynamics simulation; Myofibrillar proteins; Quartz crystal microbalance with dissipation; Salt-responsive adsorption
Substance Nomenclature: 0 (Emulsions)
0 (Fish Proteins)
0 (Muscle Proteins)
Entry Date(s): Date Created: 20250815 Date Completed: 20250916 Latest Revision: 20250916
Update Code: 20250917
DOI: 10.1016/j.foodchem.2025.145819
PMID: 40816085
Databáza: MEDLINE
Popis
Abstrakt:Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.<br />This study employed a multi-scale approach to elucidate the interfacial adsorption behavior of myofibrillar proteins (MPs) and the molecular mechanisms underlying emulsion stability under different ionic strengths. The interfacial adsorption of MPs primarily depends on electrostatic and hydrophobic interactions. When MPs approach the interface, structural changes occur, accompanied by angular deflection and orientation towards the horizontal direction. High ionic strengths (0.6-1.0 mol/L) enhance the K <subscript>diff</subscript> of MPs, with the thickness and mass of the interface film showing significant changes as ionic strength increases (1 &gt; 0.8 &gt; 0.4 &gt; 0.6 &gt; 0.2 &gt; 0). At 0.6 mol/L, the elasticity of the interface film reaches its peak, the emulsion exhibits the strongest deformation resistance, and achieves optimal stability. This discovery deepens our understanding of protein adsorption behavior at oil/water interfaces and provides new theoretical basis and methodological guidance for the practical application of MPs in the field of food emulsions.<br /> (Copyright © 2024. Published by Elsevier Ltd.)
ISSN:1873-7072
DOI:10.1016/j.foodchem.2025.145819