Changes in physicochemical and conformational properties of myofibrillar proteins isolated from mandarin fish (Siniperca chuatsi) treated by atmospheric pressure plasma jet

References

• Bedane, T. F., Chen, L., Marra, F., & Wang, S. (2017). Experimental study of radio frequency (RF) thawing of foods with movement on conveyor belt. Journal of Food Engineering, 201, 17–25. https://doi.org/10.1016/j.jfoodeng.2017.01.010
   Web of Science ®Google Scholar
• Bußler, S., Rumpold, B. A., Fröhling, A., Jander, E., Rawel, H. M., & Schlüter, O. K. (2016). Cold atmospheric pressure plasma processing of insect flour from Tenebrio molitor: Impact on microbial load and quality attributes in comparison to dry heat treatment. Innovative Food Science & Emerging Technologies, 36, 277–286. https://doi.org/10.1016/j.ifset.2016.07.002
   Web of Science ®Google Scholar
• Cai, L., Cao, M., Cao, A., Regenstein, J., Li, J., & Guan, R. (2018). Ultrasound or microwave vacuum thawing of red seabream (Pagrus major) fillets. Ultrasonics Sonochemistry, 47, 122–132. https://doi.org/10.1016/j.ultsonch.2018.05.001
   PubMed Web of Science ®Google Scholar
• Cao, Y., & 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
   PubMed Web of Science ®Google Scholar
• Chelh, I., Gatellier, P., & Sante-Lhoutellier, V. (2006). Technical note: A simplified procedure for myofibril hydrophobicity determination. Meat Science, 74(4), 681–683. https://doi.org/10.1016/j.meatsci.2006.05.019
   PubMed Web of Science ®Google Scholar
• Chen, H., Diao, J., Li, Y., Chen, Q., & Kong, B. (2016). The effectiveness of clove extracts in the inhibition of hydroxyl radical oxidation-induced structural and rheological changes in porcine myofibrillar protein. Meat Science, 111, 60–66. https://doi.org/10.1016/j.meatsci.2015.08.017
   PubMed Web of Science ®Google Scholar
• Dong, S., Wang, J. M., Cheng, L. M., Lu, Y. L., Li, S. H., & Chen, Y. (2017). Behavior of zein in aqueous ethanol under atmospheric pressure cold plasma treatment. Journal of Agricultural and Food Chemistry, 65(34), 7352–7360. https://doi.org/10.1021/acs.jafc.7b02205
   PubMed Web of Science ®Google Scholar
• Ekezie, F. C., Cheng, J. H., & Sun, D. W. (2019). Effects of atmospheric pressure plasma jet on the conformation and physicochemical properties of myofibrillar proteins from king prawn (Litopenaeus vannamei). Food Chemistry, 276, 147–156. https://doi.org/10.1016/j.foodchem.2018.09.113
   PubMed Web of Science ®Google Scholar
• Feng, X., Chen, L., Lei, N., Wang, S., Xu, X., Zhou, G., & Li, Z. (2017). Emulsifying properties of oxidatively stressed myofibrillar protein emulsion gels prepared with (-)-epigallocatechin-3-gallate and NaCl. Journal of Agricultural and Food Chemistry, 65(13), 2816–2826. https://doi.org/10.1021/acs.jafc.6b05517
   PubMed Web of Science ®Google Scholar
• Haijan, M., Chaijan, S., Panya, A., Nisoa, M., Cheong, L. Z., & Panpipat, W. (2021). High hydrogen peroxide concentration-low exposure time of plasma-activated water (PAW): A novel approach for shelf-life extension of Asian sea bass (lates calcarifer) steak. Innovative Food Science & Emerging Technologies, 74, 102861. https://doi.org/10.1016/j.ifset.2021.102861
   Web of Science ®Google Scholar
• Hu, X., Zhang, Y., Wu, R. A., Liao, X., Liu, D., Cullen, P. J., Zhou, R.-W., & Ding, T. (2021). Diagnostic analysis of reactive species in plasma-activated water (PAW): Current advances and outlooks. Journal of Physics D: Applied Physics, 55(2), 023002. https://doi.org/10.1088/1361-6463/ac286a
   Web of Science ®Google Scholar
• Huson, M. G., Strounina, E. V., Kealley, C. S., Rout, M. K., Church, J. S., Appelqvist, I. A., Gidley, M. J., & Gilbert, E. P. (2011). Effects of thermal denaturation on the solid-state structure and molecular mobility of glycinin. Biomacromolecules, 12(6), 2092–2102. https://doi.org/10.1021/bm200080h
   PubMed Web of Science ®Google Scholar
• Ji, H., Dong, S., Han, F., Li, Y., Chen, G., Li, L., & Chen, Y. (2017). Effects of dielectric barrier discharge (DBD) cold plasma treatment on physicochemical and functional properties of peanut protein. Food and Bioprocess Technology, 11(2), 344–354. https://doi.org/10.1007/s11947-017-2015-z
   Web of Science ®Google Scholar
• Jia, D., You, J., Hu, Y., Liu, R., & Xiong, S. (2015). Effect of CaCl2 on denaturation and aggregation of silver carp myosin during setting. Food Chemistry, 185, 212–218. https://doi.org/10.1016/j.foodchem.2015.03.130
   PubMed Web of Science ®Google Scholar
• Jia, G., Liu, H., Nirasawa, S., & Liu, H. (2017). Effects of high-voltage electrostatic field treatment on the thawing rate and post-thawing quality of frozen rabbit meat. Innovative Food Science & Emerging Technologies, 41, 348–356. https://doi.org/10.1016/j.ifset.2017.04.011
   Web of Science ®Google Scholar
• Jia, G., Nirasawa, S., Ji, X., Luo, Y., & Liu, H. (2018). Physicochemical changes in myofibrillar proteins extracted from pork tenderloin thawed by a high-voltage electrostatic field. Food Chemistry, 240, 910–916. https://doi.org/10.1016/j.foodchem.2017.07.138
   PubMed Web of Science ®Google Scholar
• Jia, J., Gao, X., Hao, M., & Tang, L. (2017). Comparison of binding interaction between beta-lactoglobulin and three common polyphenols using multi-spectroscopy and modeling methods. Food Chemistry, 228, 143–151. https://doi.org/10.1016/j.foodchem.2017.01.131
   PubMed Web of Science ®Google Scholar
• Kang, T., Yim, D., Kim, S. S., Baek, K. H., Kim, H. J., & Jo, C. (2022). Effect of plasma-activated acetic acid on inactivation of Salmonella typhimurium and quality traits on chicken meats. Poultry Science, 101(5), 101793. https://doi.org/10.1016/j.psj.2022.101793
   PubMed Web of Science ®Google Scholar
• LeBail, A., Chevalier, D., & Mussa, D. M. (2002). High pressure freezing and thawing of foods a review. International Journal of Refrigeration, 25(5), 504–513. https://doi.org/10.1016/S0140-7007(01)00030-5
   Web of Science ®Google Scholar
• Leygonie, C., Britz, T. J., & Hoffman, L. C. (2012). Impact of freezing and thawing on the quality of meat: Review. Meat Science, 91(2), 93–98. https://doi.org/10.1016/j.meatsci.2012.01.013
   PubMed Web of Science ®Google Scholar
• Li, F., Wang, B., Liu, Q., Chen, Q., Zhang, H., Xia, X., & Kong, B. (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
   PubMed Web of Science ®Google Scholar
• Li, K., Fu, L., Zhao, Y.-Y., Xue, S.-W., Wang, P., Xu, X.-L., & Bai, Y.-H. (2020). Use of high-intensity ultrasound to improve emulsifying properties of chicken myofibrillar protein and enhance the rheological properties and stability of the emulsion. Food Hydrocolloids, 98, 105275. https://doi.org/10.1016/j.foodhyd.2019.105275
   Web of Science ®Google Scholar
• Li, K., Liu, J. Y., Fu, L., Zhao, Y. Y., & Bai, Y. H. (2019). Comparative study of thermal gelation properties and molecular forces of actomyosin extracted from normal and pale, soft and exudative-like chicken breast meat. Asian-Australasian Journal of Animal Sciences, 32(5), 721–733. https://doi.org/10.5713/ajas.18.0389
   PubMed Web of Science ®Google Scholar
• Li, S., Zheng, Y., Xu, P., Zhu, X., & Zhou, C. (2018). L-Lysine and l-arginine inhibit myosin aggregation and interact with acidic amino acid residues of myosin: The role in increasing myosin solubility. Food Chemistry, 242, 22–28. https://doi.org/10.1016/j.foodchem.2017.09.033
   PubMed Web of Science ®Google Scholar
• Li, Y., Kong, B., Xia, X., Liu, Q., & Diao, X. (2013). Structural changes of the myofibrillar proteins in common carp (Cyprinus carpio) muscle exposed to a hydroxyl radical-generating system. Process Biochemistry, 48(5–6), 863–870. https://doi.org/10.1016/j.procbio.2013.03.015
   Web of Science ®Google Scholar
• Liao, X., Xiang, Q., Cullen, P. J., Su, Y., Chen, S., Ye, X., Liu, D., & Ding, T. (2020). Plasma-activated water (PAW) and slightly acidic electrolyzed water (SAEW) as beef thawing media for enhancing microbiological safety. LWT-Food Science and Technology, 17, 108649. https://doi.org/10.1016/j.lwt.2019.108649
   Google Scholar
• Lin, R., Xiao, X., Yue, Y., Wang, Y., Pan, D., Wang, D., Yang, Q., He, J., & Cao, J. (2020). Myosin affects the structure and volatile flavour compounds binding of G‐actin in grass carp. International Journal of Food Science & Technology, 55(10), 3235–3245. https://doi.org/10.1111/ijfs.14586
   Web of Science ®Google Scholar
• Liu, J., Cui, Y., & Liu, J. (1998). Food consumption and growth of two piscivorous fishes, the mandarin fish and the Chinese snakehead. Journal of Fish Biology, 53(5), 1071–1083. https://doi.org/10.1111/j.1095-8649.1998.tb00464.x
   Web of Science ®Google Scholar
• Liu, Q., Lu, Y., Han, J., Chen, Q., & Kong, B. (2015). Structure-modification by moderate oxidation in hydroxyl radical-generating systems promote the emulsifying properties of soy protein isolate. Food Structure, 6, 21–28. https://doi.org/10.1016/j.foostr.2015.10.001
   Google Scholar
• Lu, X., Naidis, V. G., Laroussi, M., Reuter, S., & Graves, B. D. (2016). Reactive species in non-equilibrium atmospheric-pressure plasmas: Generation, transport, and biological effects. Physics Reports, 630, 1–84. https://doi.org/10.1016/j.physrep.2016.03.003
   Google Scholar
• Luo, J., Xu, W., Liu, Q., Zou, Y., Wang, D., & Zhang, J. (2022). Dielectric barrier discharge cold plasma treatment of pork loin: Effects on muscle physicochemical properties and emulsifying properties of pork myofibrillar protein. LWT-Food Science and Technology, 162, 113484. https://doi.org/10.1016/j.lwt.2022.113484
   Web of Science ®Google Scholar
• Miao, W., Nyaisaba, B. M., Koddy, J. K., Chen, M., Hatab, S., & Deng, S. (2020). Effect of cold atmospheric plasma on the physicochemical and functional properties of myofibrillar protein from Alaska pollock (Theragra chalcogramma). International Journal of Food Science & Technology, 55, 517–525. https://doi.org/10.1111/ijfs.14295
   Web of Science ®Google Scholar
• Niu, H., Xia, X., Wang, C., Kong, B., & Liu, Q. (2018). Thermal stability and gel quality of myofibrillar protein as affected by soy protein isolates subjected to an acidic pH and mild heating. Food Chemistry, 242, 188–195. https://doi.org/10.1016/j.foodchem.2017.09.055
   PubMed Web of Science ®Google Scholar
• Oehmigen, K., Hähnel, M., Brandenburg, R., Wilke, C., Weltmann, K. D., & von Woedtke, T. (2010). The role of acidification for antimicrobial activity of atmospheric pressure plasma in liquids. Plasma Processes and Polymers, 7(3–4), 250–257. https://doi.org/10.1002/ppap.200900077
   Web of Science ®Google Scholar
• Qian, J., Wang, C., Zhuang, H., Nasiru, M. M., Zhang, J., & Yan, W. (2021a). Evaluation of meat-quality and myofibrillar protein of chicken drumsticks treated with plasma-activated lactic acid as a novel sanitizer. LWT, 138, 110642. https://doi.org/10.1016/j.lwt.2020.110642
   Web of Science ®Google Scholar
• Qian, J., Wang, Y., Zhuang, H., Yan, W., Zhang, J., & Luo, J. (2021b). Plasma activated water-induced formation of compact chicken myofibrillar protein gel structures with intrinsically antibacterial activity. Food Chemistry, 351, 129278. https://doi.org/10.1016/j.foodchem.2021.129278
   PubMed Web of Science ®Google Scholar
• Segat, A., Misra, N. N., Cullen, P. J., & Innocente, N. (2015). Atmospheric pressure cold plasma (ACP) treatment of whey protein isolate model solution. Innovative Food Science & Emerging Technologies, 29, 247–254. https://doi.org/10.1016/j.ifset.2015.03.014
   Web of Science ®Google Scholar
• Sharifian, A., Soltanizadeh, N., & Abbaszadeh, R. (2019). Effects of dielectric barrier discharge plasma on the physicochemical and functional properties of myofibrillar proteins. Innovative Food Science & Emerging Technologies, 54, 1–8. https://doi.org/10.1016/j.ifset.2019.03.006
   Web of Science ®Google Scholar
• Sun, C., Dai, L., He, X., Liu, F., Yuan, F., & Gao, Y. (2016). Effect of heat treatment on physical, structural, thermal and morphological characteristics of zein in ethanol-water solution. Food Hydrocolloids, 58, 11–19. https://doi.org/10.1016/j.foodhyd.2016.02.014
   Web of Science ®Google Scholar
• Sun, C., Niu, Y., Ye, X., Dong, J., Hu, W., Zeng, Q., Chen, Z., Tian, Y., Zhang, J., & Lu, M. (2017). Construction of a high-density linkage map and mapping of sex determination and growth-related loci in the mandarin fish (Siniperca chuatsi). BMC Genomics, 18(1), 446. https://doi.org/10.1186/s12864-017-3830-3
   PubMedGoogle Scholar
• Sun, C. F., Ye, X., Tian, Y. Y., & Dong, J. J. (2015). Simple sequence repeat-based analysis of the genetic diversity and population genetic structure of populations of siniperca chuatsi. Genetics & Molecular Research, 14(3), 9343–9352. https://doi.org/10.4238/2015.August.10.15
   PubMed Web of Science ®Google Scholar
• Traylor, M. J., Pavlovich, M. J., Karim, S., Hait, P., Sakiyama, Y., Clark, D. S., & Graves, D. B. (2011). Long-term antibacterial efficacy of air plasma-activated water. Journal of Physics D: Applied Physics, 44(47), 472001. https://doi.org/10.1088/0022-3727/44/47/472001
   Web of Science ®Google Scholar
• Wang, B., Du, X., Kong, B., Liu, Q., Li, F., Pan, N., Xia, X., & Zhang, D. (2020). Effect of ultrasound thawing, vacuum thawing, and microwave thawing on gelling properties of protein from porcine longissimus dorsi. Ultrasonics Sonochemistry, 64, 104860. https://doi.org/10.1016/j.ultsonch.2019.104860
   PubMed Web of Science ®Google Scholar
• Wang, J., Han, R., Liao, X., & Ding, T. (2021). Application of plasma-activated water (PAW) for mitigating methicillin-resistant Staphylococcus aureus (MRSA) on cooked chicken surface. LWT-Food Science and Technology, 137, 110465. https://doi.org/10.1016/j.lwt.2020.110465
   Web of Science ®Google Scholar
• Xiong, Y. L., Blanchard, S. P., Ooizumi, T., & Ma, Y. (2010). Hydroxyl radical and ferryl-generating systems promote gel network formation of myofibrillar protein. Journal of Food Science, 75(2), C215–221. https://doi.org/10.1111/j.1750-3841.2009.01511.x
   PubMed Web of Science ®Google Scholar
• Zhang, Z., Yang, Y., Zhou, P., Zhang, X., & Wang, J. (2017). Effects of high pressure modification on conformation and gelation properties of myofibrillar protein. Food Chemistry, 217, 678–686. https://doi.org/10.1016/j.foodchem.2016.09.040
   PubMed Web of Science ®Google Scholar
• Zhao, X., Bai, Y., Xing, T., Xu, X. L., & Zhou, G. (2018). Use of an isoelectric solubilization/precipitation process to modify the functional properties of PSE (pale, soft, exudative)-like chicken meat protein: A mechanistic approach. Food Chemistry, 248, 201–209. https://doi.org/10.1016/j.foodchem.2017.12.048
   PubMed Web of Science ®Google Scholar
• Zhao, X., Xing, T., Chen, X., Han, M., Deng, S., Xu, X., & Zhou, G. (2017). Changes of molecular forces during thermo-gelling of protein isolated from PSE-Like chicken breast by various isoelectric solubilization/precipitation extraction strategies. Food and Bioprocess Technology, 10(7), 1240–1247. https://doi.org/10.1007/s11947-017-1893-4
   Web of Science ®Google Scholar
• Zhao, Y. M., Ojha, S., Burgess, C. M., Sun, D. W., & Tiwari, B. K. (2020). Influence of various fish constituents on inactivation efficacy of plasma‐activated water. International Journal of Food Science & Technology, 55(6), 2630–2641. https://doi.org/10.1111/ijfs.14516
   Web of Science ®Google Scholar