Cross-linking effects of EGCG on myofibrillar protein from common carp (Cyprinus carpio) and the action mechanism
Chong Tan
Antioxidant Polyphenols Team, Department of Food Engineering, Sichuan University, Chengdu, PR China
Search for more papers by this authorQian-Da Xu
Antioxidant Polyphenols Team, Department of Food Engineering, Sichuan University, Chengdu, PR China
Search for more papers by this authorNan Chen
Antioxidant Polyphenols Team, Department of Food Engineering, Sichuan University, Chengdu, PR China
Search for more papers by this authorQiang He
The Key Laboratory of Food Science and Technology of Sichuan Province of Education, Sichuan University, Chengdu, PR China
Search for more papers by this authorQun Sun
The Key Laboratory of Food Science and Technology of Sichuan Province of Education, Sichuan University, Chengdu, PR China
Search for more papers by this authorCorresponding Author
Wei-Cai Zeng
Antioxidant Polyphenols Team, Department of Food Engineering, Sichuan University, Chengdu, PR China
The Key Laboratory of Food Science and Technology of Sichuan Province of Education, Sichuan University, Chengdu, PR China
Correspondence
Wei-Cai Zeng, Antioxidant Polyphenols Team, Department of Food Engineering, Sichuan University, Chengdu, Sichuan 610065, PR China.
Email: [email protected]
Search for more papers by this authorChong Tan
Antioxidant Polyphenols Team, Department of Food Engineering, Sichuan University, Chengdu, PR China
Search for more papers by this authorQian-Da Xu
Antioxidant Polyphenols Team, Department of Food Engineering, Sichuan University, Chengdu, PR China
Search for more papers by this authorNan Chen
Antioxidant Polyphenols Team, Department of Food Engineering, Sichuan University, Chengdu, PR China
Search for more papers by this authorQiang He
The Key Laboratory of Food Science and Technology of Sichuan Province of Education, Sichuan University, Chengdu, PR China
Search for more papers by this authorQun Sun
The Key Laboratory of Food Science and Technology of Sichuan Province of Education, Sichuan University, Chengdu, PR China
Search for more papers by this authorCorresponding Author
Wei-Cai Zeng
Antioxidant Polyphenols Team, Department of Food Engineering, Sichuan University, Chengdu, PR China
The Key Laboratory of Food Science and Technology of Sichuan Province of Education, Sichuan University, Chengdu, PR China
Correspondence
Wei-Cai Zeng, Antioxidant Polyphenols Team, Department of Food Engineering, Sichuan University, Chengdu, Sichuan 610065, PR China.
Email: [email protected]
Search for more papers by this authorAbstract
The cross-linking effects and action mechanism of epigallocatechin gallate (EGCG) on myofibrillar protein from common carp (Cyprinus carpio) were investigated. According to particle size, zeta potential, and atomic force microscopy, EGCG could cause the aggregation of myofibrillar protein, while hydrogen bonds and electrostatic interactions were the main molecular forces. With the measurement of Fourier transform infrared spectrum, surface hydrophobicity, fluorescence spectrum, circular dichroism spectrum, and molecular dynamics simulation, EGCG could make the spatial configuration of myofibrillar protein loose, enhance the exposure of amino acid residues, and further change its secondary and tertiary structures by forming intermolecular and intramolecular hydrogen bonds with myofibrillar protein. In addition, the gel properties of myofibrillar protein were improved by EGCG. All results suggested that EGCG had the cross-linking effects on myofibrillar protein in carp meat and could further improve its properties, which showed the potential to improve the qualities of fish meat in food industry.
Practical applications
Compared with other meat, fish meat is particularly easy to break and deteriorate during its processing and sales due to the short length and low cross-linking degree of fish myofibrillar protein, which shows some negative impacts on the quality of fish meat. In the present study, epigallocatechin gallate (EGCG) showed the significant cross-linking effects on carp myofibrillar protein and further improved its physicochemical properties. All results suggested that EGCG had the potential to increase the cross-linking degree of fish myofibrillar protein and improve its properties, so as to ameliorate the quality of fish meat during processing and storage.
CONFLICT OF INTEREST
The authors have declared no conflict of interest.
Open Research
DATA AVAILABILITY STATEMENT
Data sharing is not applicable to this article as no new data were created or analyzed in this study.
Supporting Information
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REFERENCES
- Bartosikova, L., & Necas, J. (2018). Epigallocatechin gallate: A review. Veterinární Medicína, 63, 443–467. https://doi.org/10.17221/31/2018-vetmed
- Benjakul, S., Visessanguan, W., Thongkaew, C., & Tanaka, M. (2003). Comparative study on physicochemical changes of muscle proteins from some tropical fish during frozen storage. Food Research International, 36, 787–795. https://doi.org/10.1016/s0963-9969(03)00073-5
- Bertram, H. C., Kohler, A., Bocker, U., Ofstad, R., & Andersen, H. J. (2006). Heat-induced changes in myofibrillar protein structures and myowater of two pork qualities. A combined FT-IR spectroscopy and low-field NMR relaxometry study. Journal of Agricultural and Food Chemistry, 54, 1740–1746. https://doi.org/10.1021/jf0514726
- Cao, Y. G., & Xiong, Y. L. (2015). Chlorogenic acid-mediated gel formation of oxidatively stressed myofibrillar protein. Food Chemistry, 180, 235–243. https://doi.org/10.1016/j.foodchem.2015.02.036
- Carocho, M., & Ferreira, I. C. F. R. (2013). A review on antioxidants, prooxidants and related controversy: Natural and synthetic compounds, screening and analysis methodologies and future perspectives. Food and Chemical Toxicology, 51, 15–25. https://doi.org/10.1016/j.fct.2012.09.021
- Chen, L., Li, C. Y., Ullah, N., Guo, Y., Sun, X. C., Wang, X. J., Xu, X. L., Hackman, R. M., Zhou, G. H., & Feng, X. C. (2016). Different physicochemical, structural and digestibility characteristics of myofibrillar protein from PSE and normal pork before and after oxidation. Meat Science, 121, 228–237. https://doi.org/10.1016/j.meatsci.2016.06.010
- Cheng, J. R., Xu, L., Xiang, R., Liu, X. M., & Zhu, M. J. (2020). Effects of mulberry polyphenols on oxidation stability of sarcoplasmic and myofibrillar proteins in dried minced pork slices during processing and storage. Meat Science, 160, 107973. https://doi.org/10.1016/j.meatsci.2019.107973
- Diao, X. Q., Guan, H. N., Zhao, X. X., Diao, X. P., & Kong, B. H. (2016). Physicochemical and structural properties of composite gels prepared with myofibrillar protein and lard diacylglycerols. Meat Science, 121, 333–341. https://doi.org/10.1016/j.meatsci.2016.07.002
- Dong, M., Tian, H. X., Xu, Y. J., Han, M. Y., & Xu, X. L. (2021). Effects of pulsed electric fields on the conformation and gelation properties of myofibrillar proteins isolated from pale, soft, exudative (PSE)-like chicken breast meat: A molecular dynamics study. Food Chemistry, 342, 128306. https://doi.org/10.1016/j.foodchem.2020.128306
- Ellman, G. L. (1959). Tissue sulfhydryl groups. Archives of Biochemistry and Biophysics, 82, 70–77. https://doi.org/10.1016/0003-9861(59)90090-6
- Gao, H. X., He, Z., Sun, Q., He, Q., & Zeng, W. C. (2019). A functional polysaccharide film forming by pectin, chitosan, and tea polyphenols. Carbohydrate Polymers, 215, 1–7. https://doi.org/10.1016/j.carbpol.2019.03.029
- Gao, H. X., Liang, H. Y., Chen, N., Shi, B., & Zeng, W. C. (2022). Potential of phenolic compounds in Ligustrum robustum (Rxob.) blume as antioxidant and lipase inhibitors: Multi-spectroscopic methods and molecular docking. Journal of Food Science, 87, 651–663. https://doi.org/10.1111/1750-3841.16020
- Gao, M. R., Xu, Q. D., & Zeng, W. C. (2020). Effect of tea polyphenols on the tenderness of yak meat. Journal of Food Processing and Preservation, 44, e14433. https://doi.org/10.1111/jfpp.14433
- Ge, G., Guo, W. X., Zheng, J. B., Zhao, M. M., & Sun, W. Z. (2021). Effect of interaction between tea polyphenols with soymilk protein on inactivation of soybean trypsin inhibitor. Food Hydrocolloids, 111, 106177. https://doi.org/10.1016/j.foodhyd.2020.106177
- Ge, G., Han, Y. R., Zheng, J. B., Zhao, M. M., & Sun, W. Z. (2020). Physicochemical characteristics and gel-forming properties of myofibrillar protein in an oxidative system affected by partial substitution of NaCl with KCl, MgCl2 or CaCl2. Food Chemistry, 309, 125614. https://doi.org/10.1016/j.foodchem.2019.125614
- Gómez-Guillén, M. C., Montero, P., Solas, M. T., & Borderías, A. J. (1998). Thermally Induced aggregation of giant squid (Dosidicus gigas) mantle proteins. Physicochemical contribution of added ingredients. Journal of Agricultural and Food Chemistry, 46, 3440–3446. https://doi.org/10.1021/jf9801116
- Guo, A. Q., Jiang, J., True, A. D., & Xiong, Y. L. (2021). Myofibrillar protein cross-linking and gelling behavior modified by structurally relevant phenolic compounds. Journal of Agricultural and Food Chemistry, 69, 1308–1317. https://doi.org/10.1021/acs.jafc.0c04365
- Jia, D., Huang, Q. L., & Xiong, S. B. (2016). Chemical interactions and gel properties of black carp actomyosin affected by MTGase and their relationships. Food Chemistry, 196, 1180–1187. https://doi.org/10.1016/j.foodchem.2015.10.030
- Jia, N., Zhang, F. X., Liu, Q., Wang, L. T., Lin, S. W., & Liu, D. Y. (2019). The beneficial effects of rutin on myofibrillar protein gel properties and related changes in protein conformation. Food Chemistry, 301, 125206. https://doi.org/10.1016/j.foodchem.2019.125206
- Kang, Z. L., Zhang, X. H., Li, X., Song, Z. J., Ma, H. J., Lu, F., Zhu, M. M., Zhao, S. M., & Wang, Z. R. (2020). The effects of sodium chloride on proteins aggregation, conformation and gel properties of pork myofibrillar protein running head: Relationship aggregation, conformation and gel properties. Journal of Food Science and Technology, 58, 2258–2264. https://doi.org/10.1007/s13197-020-04736-4
- King, L., & Lehrer, S. S. (1989). Thermal unfolding of myosin rod and light meromyosin: Circular dichroism and tryptophan fluorescence studies. Biochemistry, 28, 3498–3502. https://doi.org/10.1021/bi00434a052
- Kobayashi, Y., Mayer, S. G., & Park, J. W. (2017). FT-IR and Raman spectroscopies determine structural changes of tilapia fish protein isolate and surimi under different comminution conditions. Food Chemistry, 226, 156–164. https://doi.org/10.1016/j.foodchem.2017.01.068
- Li, F. F., Wang, B., Liu, Q., Chen, Q., Zhang, H. W., Xia, X. F., & Kong, B. H. (2019). Changes in myofibrillar protein gel quality of porcine longissimus muscle induced by its structural modification under different thawing methods. Meat Science, 147, 108–115. https://doi.org/10.1016/j.meatsci.2018.09.003
- Li, M., Yang, R., Feng, X. C., Fan, X. J., Liu, Y. P., Xu, X. L., Zhou, G. H., Zhu, B. W., Ullah, N., & Chen, L. (2022). Effects of low-frequency and high-intensity ultrasonic treatment combined with curdlan gels on the thermal gelling properties and structural properties of soy protein isolate. Food Hydrocolloids, 127, 107506. https://doi.org/10.1016/j.foodhyd.2022.107506
- Li, X. X., Ma, Y. Y., Sun, P., Liu, H. Y., Cai, L. Y., & Li, J. R. (2020). Effect of ultrasonic thawing on protein properties and muscle quality of bonito. Journal of Food Processing and Preservation, 45, e14930. https://doi.org/10.1111/jfpp.14930
- Liu, R., Zhao, S. M., Xiong, S. B., Die, B. J., & Qin, L. H. (2008). Role of secondary structures in the gelation of porcine myosin at different pH values. Meat Science, 80, 632–639. https://doi.org/10.1016/j.meatsci.2008.02.014
- Medina-Vivanco, M., Sobral, P. J. Á., Sereno, A. M., & Hubinger, M. D. (2007). Denaturation and the glass transition temperatures of myofibrillar proteins from osmotically dehydrated tilapia: Effect of sodium chloride and sucrose. International Journal of Food Properties, 10, 791–805. https://doi.org/10.1080/10942910601185184
- Mehranfar, F., Bordbar, A.-K., & Parastar, H. (2013). A combined spectroscopic, molecular docking and molecular dynamic simulation study on the interaction of quercetin with β-casein nanoparticles. Journal of Photochemistry and Photobiology B: Biology, 127, 100–107. https://doi.org/10.1016/j.jphotobiol.2013.07.019
- Qiu, C. J., Xia, W. S., & Jiang, Q. X. (2014). Pressure-induced changes of silver carp (Hypophthalmichthys molitrix) myofibrillar protein structure. European Food Research and Technology, 238, 753–761. https://doi.org/10.1007/s00217-014-2155-6
- Ramirez-Suarez, J. C., Xiong, Y. L., & Wang, B. (2001). Tranglutaminase cross-linking of bovine cardiac myofibrillar proteins and its effect on protein gelation. Journal of Muscle Foods, 12, 85–96. https://doi.org/10.1111/j.1745-4573.2001.tb00301.x
- Roy, A. S., Dinda, A. K., Chaudhury, S., & Dasgupta, S. (2014). Binding of antioxidant flavonol morin to the native state of bovine serum albumin: Effects of urea and metal ions on the binding. Journal of Luminescence, 145, 741–751. https://doi.org/10.1016/j.jlumin.2013.08.054
- Strauss, G., & Gibson, S. M. (2004). Plant phenolics as cross-linkers of gelatin gels and gelatin-based coacervates for use as food ingredients. Food Hydrocolloids, 18, 81–89. https://doi.org/10.1016/s0268-005x(03)00045-6
- Sun, W. Z., Li, Q. Y., Zhou, F. B., Zhao, H. F., & Zhao, M. M. (2014). Surface characterization of oxidized myofibrils using X-ray photoelectron spectroscopy and scanning electron microscopy. Journal of Agricultural and Food Chemistry, 62, 7507–7514. https://doi.org/10.1021/jf501272p
- Tang, C. H., Sun, X., Yin, S. W., & Ma, C. Y. (2008). Transglutaminase-induced cross-linking of vicilin-rich kidney protein isolate: Influence on the functional properties and in vitro digestibility. Food Research International, 41, 941–947. https://doi.org/10.1016/j.foodres.2008.07.015
- Wang, H., Luo, Y. K., Shi, C., & Shen, H. X. (2015). Effect of different thawing methods and multiple freeze-thaw cycles on the quality of common carp (Cyprinus carpio). Journal of Aquatic Food Product Technology, 24, 153–162. https://doi.org/10.1080/10498850.2013.763884
- Wang, S. H., Sun, Z. Y., Dong, S. Z., Liu, Y., & Liu, Y. (2014). Molecular Interactions between (−)-epigallocatechin gallate analogs and pancreatic lipase. PLoS One, 9, e111143. https://doi.org/10.1371/journal.pone.0111143
- Xu, Q. D., Yu, Z. L., & Zeng, W. C. (2021). Structural and functional modifications of myofibrillar protein by natural phenolic compounds and their application in pork meatball. Food Research International, 148, 110593. https://doi.org/10.1016/j.foodres.2021.110593
- Zeng, W. C., Zhang, Z., & Jia, L. R. (2014). Antioxidant activity and characterization of antioxidant polysaccharides from pine needle (Cedrus deodara). Carbohydrate Polymers, 108, 58–64. https://doi.org/10.1016/j.carbpol.2014.03.022
- Zhang, Z. Y., Yang, Y. L., Tang, X. Z., Chen, Y. J., & You, Y. (2015). Effects of ionic strength on chemical forces and functional properties of heat-induced myofibrillar protein gel. Food Science and Technology Research, 21, 597–605. https://doi.org/10.3136/fstr.21.597
- Zhao, Y. Y., Zhou, G. H., & Zhang, W. G. (2019). Effects of regenerated cellulose fiber on the characteristics of myofibrillar protein gels. Carbohydrate Polymers, 209, 276–281. https://doi.org/10.1016/j.carbpol.2019.01.042
- Zhou, Z. Q., Xu, Q. D., Chen, L., Chen, N., Gao, H. X., Sun, Q., & Zeng, W. C. (2021). Interaction and action mechanism of quercetin and myofibrillar protein and its effects on the quality of cured meat. Journal of Food Processing and Preservation, 45, 16020. https://doi.org/10.1111/jfpp.16020