Yangyang Feng , Xin Li , Zihan Zhao , Baohua Kong , Chuanai Cao , Fangda Sun , Qian Liu , Xinning Huang
{"title":"基于构象变化、流变行为和分子对接的微生物转谷氨酰胺酶介导的肌纤维蛋白和κ-卡拉胶混合溶胶中相互作用的基础","authors":"Yangyang Feng , Xin Li , Zihan Zhao , Baohua Kong , Chuanai Cao , Fangda Sun , Qian Liu , Xinning Huang","doi":"10.1016/j.foodhyd.2025.111253","DOIUrl":null,"url":null,"abstract":"<div><div>The influence of transglutaminase (TG) on the interactional behaviour between myofibrillar protein (MP) and <em>κ</em>-carrageenan (KC) was investigated based on conformational alterations, rheological behavior and molecular docking. The results indicated that the addition of TG or KC obviously decreased the solubility of MP, resulting in a decrease in the fluidity and uniformity of MP sol, but increased the turbidity and surface hydrophobicity of mixed sols (<em>P</em> < 0.05). Meanwhile, an appropriate TG concentration promoted the interaction between MP and KC via hydrophobic interaction and hydrogen bonds and induced protein conformational transformation from α-helix to β-sheet (<em>P</em> < 0.05). Moreover, ultraviolet and fluorescence spectra demonstrated that TG incorporation changed the microenvironment of the aromatic amino acids in MP and increasingly protected them from the fluorescence-quenching effect of KC. Furthermore, microscopic observations revealed that TG-induced protein aggregation gradually intensified with increasing TG concentration and was attenuated in the presence of KC. At a TG concentration of 0.3%, the protein distribution within the MP–KC mixed sol was more uniform and exhibited a weak network structure, possibly explaining the synergistic effect of TG and KC on improving the apparent viscosity, dynamic viscoelasticity and mechanical properties (e.g., firmness, consistency, cohesiveness, and viscosity) of the mixed sols. Additionally, the molecular docking and molecular dynamics (MD) simulation results suggested that van der Waals, electrostatic, and nonpolar solvation energy all help maintain the stability of the interactions of myosin with KC and TG. However, the positive polar solvation energy was not conducive to the stability of the mixed systems. These findings potentially provide a more comprehensive understanding of the TG-mediated interactional behaviour in MP–KC sols.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"165 ","pages":"Article 111253"},"PeriodicalIF":11.0000,"publicationDate":"2025-02-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Underlying the interactions in myofibrillar proteins and κ-carrageenan mixed sols as mediated by microbial transglutaminase based on conformational alterations, rheological behavior and molecular docking\",\"authors\":\"Yangyang Feng , Xin Li , Zihan Zhao , Baohua Kong , Chuanai Cao , Fangda Sun , Qian Liu , Xinning Huang\",\"doi\":\"10.1016/j.foodhyd.2025.111253\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><div>The influence of transglutaminase (TG) on the interactional behaviour between myofibrillar protein (MP) and <em>κ</em>-carrageenan (KC) was investigated based on conformational alterations, rheological behavior and molecular docking. The results indicated that the addition of TG or KC obviously decreased the solubility of MP, resulting in a decrease in the fluidity and uniformity of MP sol, but increased the turbidity and surface hydrophobicity of mixed sols (<em>P</em> < 0.05). Meanwhile, an appropriate TG concentration promoted the interaction between MP and KC via hydrophobic interaction and hydrogen bonds and induced protein conformational transformation from α-helix to β-sheet (<em>P</em> < 0.05). Moreover, ultraviolet and fluorescence spectra demonstrated that TG incorporation changed the microenvironment of the aromatic amino acids in MP and increasingly protected them from the fluorescence-quenching effect of KC. Furthermore, microscopic observations revealed that TG-induced protein aggregation gradually intensified with increasing TG concentration and was attenuated in the presence of KC. At a TG concentration of 0.3%, the protein distribution within the MP–KC mixed sol was more uniform and exhibited a weak network structure, possibly explaining the synergistic effect of TG and KC on improving the apparent viscosity, dynamic viscoelasticity and mechanical properties (e.g., firmness, consistency, cohesiveness, and viscosity) of the mixed sols. Additionally, the molecular docking and molecular dynamics (MD) simulation results suggested that van der Waals, electrostatic, and nonpolar solvation energy all help maintain the stability of the interactions of myosin with KC and TG. However, the positive polar solvation energy was not conducive to the stability of the mixed systems. These findings potentially provide a more comprehensive understanding of the TG-mediated interactional behaviour in MP–KC sols.</div></div>\",\"PeriodicalId\":320,\"journal\":{\"name\":\"Food Hydrocolloids\",\"volume\":\"165 \",\"pages\":\"Article 111253\"},\"PeriodicalIF\":11.0000,\"publicationDate\":\"2025-02-19\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Food Hydrocolloids\",\"FirstCategoryId\":\"97\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S0268005X25002139\",\"RegionNum\":1,\"RegionCategory\":\"农林科学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"CHEMISTRY, APPLIED\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Food Hydrocolloids","FirstCategoryId":"97","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0268005X25002139","RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"CHEMISTRY, APPLIED","Score":null,"Total":0}
Underlying the interactions in myofibrillar proteins and κ-carrageenan mixed sols as mediated by microbial transglutaminase based on conformational alterations, rheological behavior and molecular docking
The influence of transglutaminase (TG) on the interactional behaviour between myofibrillar protein (MP) and κ-carrageenan (KC) was investigated based on conformational alterations, rheological behavior and molecular docking. The results indicated that the addition of TG or KC obviously decreased the solubility of MP, resulting in a decrease in the fluidity and uniformity of MP sol, but increased the turbidity and surface hydrophobicity of mixed sols (P < 0.05). Meanwhile, an appropriate TG concentration promoted the interaction between MP and KC via hydrophobic interaction and hydrogen bonds and induced protein conformational transformation from α-helix to β-sheet (P < 0.05). Moreover, ultraviolet and fluorescence spectra demonstrated that TG incorporation changed the microenvironment of the aromatic amino acids in MP and increasingly protected them from the fluorescence-quenching effect of KC. Furthermore, microscopic observations revealed that TG-induced protein aggregation gradually intensified with increasing TG concentration and was attenuated in the presence of KC. At a TG concentration of 0.3%, the protein distribution within the MP–KC mixed sol was more uniform and exhibited a weak network structure, possibly explaining the synergistic effect of TG and KC on improving the apparent viscosity, dynamic viscoelasticity and mechanical properties (e.g., firmness, consistency, cohesiveness, and viscosity) of the mixed sols. Additionally, the molecular docking and molecular dynamics (MD) simulation results suggested that van der Waals, electrostatic, and nonpolar solvation energy all help maintain the stability of the interactions of myosin with KC and TG. However, the positive polar solvation energy was not conducive to the stability of the mixed systems. These findings potentially provide a more comprehensive understanding of the TG-mediated interactional behaviour in MP–KC sols.
期刊介绍:
Food Hydrocolloids publishes original and innovative research focused on the characterization, functional properties, and applications of hydrocolloid materials used in food products. These hydrocolloids, defined as polysaccharides and proteins of commercial importance, are added to control aspects such as texture, stability, rheology, and sensory properties. The research's primary emphasis should be on the hydrocolloids themselves, with thorough descriptions of their source, nature, and physicochemical characteristics. Manuscripts are expected to clearly outline specific aims and objectives, include a fundamental discussion of research findings at the molecular level, and address the significance of the results. Studies on hydrocolloids in complex formulations should concentrate on their overall properties and mechanisms of action, while simple formulation development studies may not be considered for publication.
The main areas of interest are:
-Chemical and physicochemical characterisation
Thermal properties including glass transitions and conformational changes-
Rheological properties including viscosity, viscoelastic properties and gelation behaviour-
The influence on organoleptic properties-
Interfacial properties including stabilisation of dispersions, emulsions and foams-
Film forming properties with application to edible films and active packaging-
Encapsulation and controlled release of active compounds-
The influence on health including their role as dietary fibre-
Manipulation of hydrocolloid structure and functionality through chemical, biochemical and physical processes-
New hydrocolloids and hydrocolloid sources of commercial potential.
The Journal also publishes Review articles that provide an overview of the latest developments in topics of specific interest to researchers in this field of activity.