Electrostatic field; Myosin; pH value; Protein function; Protein structure; Control groups; Field groups; Functional properties; Protein functions; Proteins structures; Structure property; Sulfhydryl groups; Surface hydrophobicity; Food Science; Chemistry (all); Industrial and Manufacturing Engineering
Résumé :
[en] In this study, the effects of electrostatic field on myosin structure and function at different pH values were investigated. The results demonstrated that a higher surface hydrophobicity and lower sulfhydryl group content of the electrostatic field (EF) group compared to Control group (P < 0.05). The particle size, secondary structure, and microstructure investigations revealed that the EF group had decreased protein aggregation and a more stable protein structure. Furthermore, the application of electrostatic field improved the water holding capacity (WHC) of myosin gel by enhancing interaction between water molecules and protein, reducing the loss of free and immobilized water. In addition, the structure of the gel formed by electrostatic field was more stable, showing higher gel hardness and dense microstructure. The study further revealed that the internal mechanism of electrostatic field to maintain the quality of fresh meat may be related to maintaining the structural and functional activity of myosin.
Disciplines :
Sciences des denrées alimentaires
Auteur, co-auteur :
Xu, Yuqian ; Université de Liège - ULiège > TERRA Research Centre ; Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences, Key Laboratory of Agro-Products Quality and Safety Control in Storage and Transport Process, Ministry of Agriculture and Rural Affairs, Beijing, China
Leng, Dongmei; Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences, Key Laboratory of Agro-Products Quality and Safety Control in Storage and Transport Process, Ministry of Agriculture and Rural Affairs, Beijing, China
Schroyen, Martine ; Université de Liège - ULiège > TERRA Research Centre > Animal Sciences (AS)
Li, Xin; Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences, Key Laboratory of Agro-Products Quality and Safety Control in Storage and Transport Process, Ministry of Agriculture and Rural Affairs, Beijing, China
Wang, Debao; Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences, Key Laboratory of Agro-Products Quality and Safety Control in Storage and Transport Process, Ministry of Agriculture and Rural Affairs, Beijing, China
Zhang, Dequan; Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences, Key Laboratory of Agro-Products Quality and Safety Control in Storage and Transport Process, Ministry of Agriculture and Rural Affairs, Beijing, China
Hou, Chengli; Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences, Key Laboratory of Agro-Products Quality and Safety Control in Storage and Transport Process, Ministry of Agriculture and Rural Affairs, Beijing, China
Langue du document :
Anglais
Titre :
Structure and functional properties of myosin induced by electrostatic fields at different pH values
This work was supported by the Key R&D Program of Shandong Province, China (2023CXGC010708). The authors appreciate the assistance by Mrs. Yanli Sun and Mrs. Ying Wang of the Electron Microscope Center and Mrs. Chunhong Li and Lan Tian of the National Key Laboratory of Argo-products Processing, Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences.
Chen, C., Liu, Z., Xiong, W., Yao, Y., Li, J., Wang, L., Effect of alkaline treatment duration on rapeseed protein during pH-shift process: Unveiling physicochemical properties and enhanced emulsifying performance. Food Chemistry, 459, 2024, 140280, 10.1016/j.foodchem.2024.140280.
Chen, H., Zou, Y., Zhou, A., Liu, X., Benjakul, S., Elucidating the molecular mechanism of water migration in myosin gels of Nemipterus virgatus during low pressure coupled with heat treatment. International Journal of Biological Macromolecules, 253, 2023, 126815, 10.1016/j.ijbiomac.2023.126815.
Deng, Y., Wang, R., Xu, M., Li, X., Zhang, Y., Gooneratne, R., Li, J., Elucidating the binding mechanism of silver carp myosin to T-2 toxin using multi-spectroscopic analysis, molecular docking and molecular dynamics simulation. LWT, 117532, 2025, 10.1016/j.lwt.2025.117532.
Guo, Z., Li, Z., Wang, J., Zheng, B., Gelation properties and thermal gelling mechanism of golden threadfin bream myosin containing CaCl2 induced by high pressure processing. Food Hydrocolloids 95 (2019), 43–52, 10.1016/j.foodhyd.2019.04.017.
Han, G., Li, Y., Liu, Q., Chen, Q., Liu, H., Kong, B., Improved water solubility of myofibrillar proteins by ultrasound combined with glycation: A study of myosin molecular behavior. Ultrasonics Sonochemistry, 89, 2022, 106140, 10.1016/j.ultsonch.2022.106140.
Hartvig, R.A., van de Weert, M., Østergaard, J., Jorgensen, L., Jensen, H., Protein adsorption at charged surfaces: The role of electrostatic interactions and interfacial charge regulation. Langmuir 27:6 (2011), 2634–2643, 10.1021/la104720n.
Jia, G., Nirasawa, S., Ji, X., Luo, Y., Liu, H., Physicochemical changes in myofibrillar proteins extracted from pork tenderloin thawed by a high-voltage electrostatic field. Food Chemistry 240 (2018), 910–916, 10.1016/j.foodchem.2017.07.138.
Li, S., Zhang, K., Wu, Y., Chen, Q., Li, M., Kong, B., Zhang, C., Role of ultrasonic freezingtreated pork dumpling filling during frozen storage: Insights from protein oxidation, aggregation, and functional properties. International Journal of Refrigeration 165 (2024), 223–232, 10.1016/j.ijrefrig.2024.05.035.
Lin, H., Wang, J., Chisoro, P., Wu, G., Zhao, S., Hu, X., Yang, C., Liu, Y., Jia, W., Li, Q., Zhang, C., Blecker, C., Li, X., Changes in freezing parameters and temperature distribution of beef induced by AC electric field: Alleviation on freezing damage and myowater loss. Journal of Food Engineering, 387, 2025, 112343, 10.1016/j.jfoodeng.2024.112343.
Liu, M., Wei, Y., Li, X., Quek, S.Y., Zhao, J., Zhong, H., Liu, Y., Quantitative phosphoproteomic analysis of caprine muscle with high and low meat quality. Meat Science 141 (2018), 103–111, 10.1016/j.meatsci.2018.01.001.
Liu, P., Hou, M., Yue, Y., Tong, Y., Zhang, T., Lu, Z., Yang, L., Effects of ultrahigh magnetic field on the structure and properties of whey protein. LWT, 177, 2023, 114590, 10.1016/j.lwt.2023.114590.
Liu, Q., Yang, Q., Wang, Y., Jiang, Y., Chen, H., Pretreatment with low-frequency magnetic fields can improve the functional properties of pea globulin amyloid-like fibrils. Food Chemistry, 439, 2024, 138135, 10.1016/j.foodchem.2023.138135.
Liu, R., Zhao, S., Liu, Y., Yang, H., Xiong, S., Xie, B., Qin, L., Effect of pH on the gel properties and secondary structure of fish myosin. Food Chemistry 121:1 (2010), 196–202, 10.1016/j.foodchem.2009.12.030.
Liu, R., Zhao, S., Xiong, S., Xie, B., Qin, L., Role of secondary structures in the gelation of porcine myosin at different pH values. Meat Science 80:3 (2008), 632–639, 10.1016/j.meatsci.2008.02.014.
Liu, Y.-F., Oey, I., Bremer, P., Silcock, P., Carne, A., Proteolytic pattern, protein breakdown and peptide production of ovomucin-depleted egg white processed with heat or pulsed electric fields at different pH. Food Research International 108 (2018), 465–474, 10.1016/j.foodres.2018.03.075.
Müller, W.A., Sarkis, J.R., Marczak, L.D.F., Muniz, A.R., Molecular dynamics study of the effects of static and oscillating electric fields in ovalbumin. Innovative Food Science & Emerging Technologies, 75, 2022, 102911, 10.1016/j.ifset.2021.102911.
Pereira, R.N., Rodrigues, R., Avelar, Z., Leite, A.C., Leal, R., Pereira, R.S., Vicente, A., Electrical fields in the processing of protein-based foods. Foods, 13(4), 2024, 4, 10.3390/foods13040577.
Qian, S., Li, X., Wang, H., Mehmood, W., Zhong, M., Zhang, C., Blecker, C., Effects of low voltage electrostatic field thawing on the changes in physicochemical properties of myofibrillar proteins of bovine longissimus dorsi muscle. Journal of Food Engineering 261 (2019), 140–149, 10.1016/j.jfoodeng.2019.06.013.
Rodrigues, R.M., Avelar, Z., Machado, L., Pereira, R.N., Vicente, A.A., Electric field effects on proteins – Novel perspectives on food and potential health implications. Food Research International, 137, 2020, 109709, 10.1016/j.foodres.2020.109709.
Rodrigues, R.M., Vicente, A.A., Petersen, S.B., Pereira, R.N., Electric field effects on β-lactoglobulin thermal unfolding as a function of pH – Impact on protein functionality. Innovative Food Science & Emerging Technologies 52 (2019), 1–7, 10.1016/j.ifset.2018.11.010.
Sun, H., Zhang, Y., Sun, J., Dietary inulin supplementation improves the physicochemical and gel properties of duck myofibrillar protein: Insights into the effect of muscle fiber types. Food Hydrocolloids, 150, 2024, 109722, 10.1016/j.foodhyd.2023.109722.
Sun, Y., Ma, L., Fu, Y., Dai, H., Zhang, Y., The improvement of gel and physicochemical properties of porcine myosin under low salt concentrations by pulsed ultrasound treatment and its mechanism. Food Research International, 141, 2021, 110056, 10.1016/j.foodres.2020.110056.
Walayat, N., Wei, R., Su, Z., Lorenzo, J.M., Nawaz, A., Effect of tea polysaccharides on fluctuated frozen storage impaired total sulfhydryl level and structural attributes of silver carp surimi proteins. Food Hydrocolloids, 157, 2024, 110448, 10.1016/j.foodhyd.2024.110448.
Walayat, N., Xiong, Z., Xiong, H., Moreno, H.M., Niaz, N., Ahmad, M.N., Wang, P.-K., Cryoprotective effect of egg white proteins and xylooligosaccharides mixture on oxidative and structural changes in myofibrillar proteins of Culter alburnus during frozen storage. International Journal of Biological Macromolecules 158 (2020), 865–874, 10.1016/j.ijbiomac.2020.04.093.
Wang, Q., Li, Y., Sun, D.-W., Zhu, Z., Enhancing food processing by pulsed and high voltage electric fields: Principles and applications. Critical Reviews in Food Science and Nutrition 58:13 (2018), 2285–2298, 10.1080/10408398.2018.1434609.
Wang, W., Lin, H., Guan, W., Song, Y., He, X., Zhang, D., Effect of static magnetic field-assisted thawing on the quality, water status, and myofibrillar protein characteristics of frozen beef steaks. Food Chemistry, 436, 2024, 137709, 10.1016/j.foodchem.2023.137709.
Wen, H., Zhang, D., Ning, Z., Li, Z., Zhang, Y., Liu, J., Yu, T., Zhang, T., Effect of benzoic acid-based and cinnamic acid-based polyphenols on foaming properties of ovalbumin at acidic, neutral and alkaline pH conditions. Food Hydrocolloids, 153, 2024, 109998, 10.1016/j.foodhyd.2024.109998.
Wen, X., Mu, Z., Gantumur, M.-A., Bilawal, A., Jiang, Z., Zhang, L., Characterization of whey protein isolate aggregation induced by different acidic substances: Triggered by disulfide bond formation and recombination. Food Hydrocolloids, 157, 2024, 110414, 10.1016/j.foodhyd.2024.110414.
Xie, Y., Chen, B., Guo, J., Nie, W., Zhou, H., Li, P., Zhou, K., Xu, B., Effects of low voltage electrostatic field on the microstructural damage and protein structural changes in prepared beef steak during the freezing process. Meat Science, 179, 2021, 108527, 10.1016/j.meatsci.2021.108527.
Xie, Y., Liao, C., Zhou, J., Effects of external electric fields on lysozyme adsorption by molecular dynamics simulations. Biophysical Chemistry 179 (2013), 26–34, 10.1016/j.bpc.2013.05.002.
Xie, Y., Zhou, K., Chen, B., Ma, Y., Tang, C., Li, P., Wang, Z., Xu, F., Li, C., Zhou, H., Xu, B., Mechanism of low-voltage electrostatic fields on the water-holding capacity in frozen beef steak: Insights from myofilament lattice arrays. Food Chemistry, 428, 2023, 136786, 10.1016/j.foodchem.2023.136786.
Xie, Y., Zhou, K., Chen, B., Wang, Y., Nie, W., Wu, S., Wang, W., Li, P., Xu, B., Applying low voltage electrostatic field in the freezing process of beef steak reduced the loss of juiciness and textural properties. Innovative Food Science & Emerging Technologies, 68, 2021, 102600, 10.1016/j.ifset.2021.102600.
Xu, Y., Leng, D., Li, X., Wang, D., Chai, X., Schroyen, M., Zhang, D., Hou, C., Effects of different electrostatic field intensities assisted controlled freezing point storage on water holding capacity of fresh meat during the early postmortem period. Food Chemistry, 439, 2024, 138096, 10.1016/j.foodchem.2023.138096.
Xu, Y., Zhang, D., Xie, F., Li, X., Schroyen, M., Chen, L., Hou, C., Changes in water holding capacity of chilled fresh pork in controlled freezing-point storage assisted by different modes of electrostatic field action. Meat Science, 204, 2023, 109269, 10.1016/j.meatsci.2023.109269.
Yang, C., Wu, G., Liu, Y., Li, Y., Zhang, C., Liu, C., Li, X., Low-voltage electrostatic field enhances the frozen force of −12°C to suppress oxidative denaturation of the lamb protein during the subsequent frozen storage process after finishing initial freezing. Food Chemistry, 438, 2024, 138055, 10.1016/j.foodchem.2023.138055.
Yu, C., Chen, L., Xu, M., Ouyang, K., Chen, H., Lin, S., Wang, W., The effect of pH and heating on the aggregation behavior and gel properties of beef myosin. LWT, 191, 2024, 115615, 10.1016/j.lwt.2023.115615.
Yu, Q., Hong, H., Liu, Y., Monto, A.R., Gao, R., Bao, Y., Oxidation affects pH buffering capacity of myofibrillar proteins via modification of histidine residue and structure of myofibrillar proteins. International Journal of Biological Macromolecules, 260, 2024, 129532, 10.1016/j.ijbiomac.2024.129532.
Yu, S., Yan, J.-K., Jin, M.-Y., Li, L.-Q., Yu, Y.-H., Xu, L., Preparation, physicochemical and functional characterization of pectic polysaccharides from fresh passion fruit peel by magnetic-induced electric field-assisted three-phase partitioning. Food Hydrocolloids, 156, 2024, 110292, 10.1016/j.foodhyd.2024.110292.
Zhang, A., Chen, S., Wang, Y., Zhou, G., Wang, L., Wang, X., Xu, N., Effect of different homogenization pressure on soy protein isolate-vitamin D3 complex. Process Biochemistry 87 (2019), 145–150, 10.1016/j.procbio.2019.09.011.
Zhang, Y., Lyu, H., Wang, Y., Bai, G., Wang, J., Teng, W., Wang, W., Cao, J., Optimizing the formation of myosin/high-density lipoprotein composite gels: PH-dependent effects on heat-induced aggregation. International Journal of Biological Macromolecules, 268, 2024, 131786, 10.1016/j.ijbiomac.2024.131786.
Zhao, X., Han, G., Sun, Q., Liu, H., Liu, Q., Kong, B., Influence of lard-based diacylglycerol on the rheological and physicochemical properties of thermally induced pork myofibrillar protein gels at different pH levels. LWT, 117, 2020, 108708, 10.1016/j.lwt.2019.108708.
Zhou, F., Zhao, M., Cui, C., Sun, W., Influence of linoleic acid-induced oxidative modifications on physicochemical changes and in vitro digestibility of porcine myofibrillar proteins. LWT 61:2 (2015), 414–421, 10.1016/j.lwt.2014.12.037.
Zhou, Y., Yang, H., Enhancing tilapia fish myosin solubility using proline in low ionic strength solution. Food Chemistry, 320, 2020, 126665, 10.1016/j.foodchem.2020.126665.
