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• TMT technology was used to analyze the quality-related proteins in fillets
• Most DAPs are related to signal transduction mechanisms
• 8 highly correlated DAPs could be the potential biomarkers for fillets quality
• MAP had good preservation of golden pompano fillets under superchilling storage
Here, we aimed to study the changes in proteome of golden pompano fillets during post-mortem storage. Tandem mass tags (TMT) -labeled quantitative proteomic strategy was applied to investigate the relationships between protein changes and quality characteristics of modified atmosphere packaging (MAP) fillets during superchilling (-3 °C) storage. Scanning electron microscopy was used to show that the muscle histology microstructure of fillets was damaged to varying degrees, and low-field nuclear magnetic resonance was used to indf that the immobilized water and free water in the muscle of fillets changed significantly. Total sulfhydryl content, TCA-soluble peptides and Ca2+-ATPase activity also showed that the fillet protein had a deterioration by oxidation and denaturation. The Fresh (FS), MAP, and air packaging (AP) groups were set. Total of 150 proteins were identified as differential abundant proteins (DAPs) in MAP/FS, while 209 DAPs were in AP/FS group. The KEGG pathway analysis indicated that most DAPs were involved in binding proteins and protein turnover. Correlation analysis found that 52 DAPs were correlated with quality traits. Among them, 8 highly correlated DAPs are expected to be used as potential quality markers for protein oxidation and water-holding capacity. These results provide a further understanding of the muscle deterioration mechanism of packaging golden pompano fillets during superchilling.
P. Li, L. Zhou, S. Ni, et al., Establishment and characterization of a novel cell line from the brain of golden pompano (Trachinotus ovatus), In vitro Cell. Developm. Bio.-Animal 52(4) (2016) 410-418. https://doi.org/10.1007/s11626-015-9988-6.
X. Qiu, S. Chen, G. Liu, et al., Characterization of farmed ovate pompano (Trachinotus ovatus Linnaeus) freshness during ice storage by monitoring the changes of volatile profile, Food Sci. Techn. Res. 20(1) (2014) 79-84. https://doi.org/10.3136/fstr.20.79.
R. Banerjee, N. Maheswarappa, Superchilling of muscle foods: potential alternative for chilling and freezing, Cri. Rev. Food Sci. Nutrit. 59 (2017). https://doi.org/10.1080/10408398.2017.1401975.
L. Chen, D. Jiao, H. Liu, et al., Effects of water distribution and protein degradation on the texture of high pressure-treated shrimp (Penaeus monodon) during chilled storage, Food Control 132 (2022) 108555. https://doi.org/10.1016/j.foodcont.2021.108555.
C. Pan, K. Sun, X. Yang, et al., Insights on Litopenaeus vannamei quality deterioration during partial freezing storage from combining traditional quality studies and label-free based proteomic analysis, J. Food Comp. Anal. 112 (2022) 104655. https://doi.org/10.1016/j.jfca.2022.104655.
L. Qiu, M. Zhang, J. Tang, et al., Innovative technologies for producing and preserving intermediate moisture foods: a review, Food Res. Int. 116 (2019) 90-102. https://doi.org/10.1016/j.foodres.2018.12.055.
X. Zhang, C. Pan, S. Chen, et al., Effects of modified atmosphere packaging with different gas ratios on the quality changes of golden pompano (Trachinotus ovatus) fillets during superchilling storage, Foods 11(13) (2022) 1943. https://doi.org/10.3390/foods11131943.
M. Sivertsvik, J.T. Rosnes, G.H. Kleiberg, Effect of modified atmosphere packaging and superchilled storage on the microbial and sensory quality of atlantic salmon (Salmo salar) fillets, J. Food Sci. 68(4) (2003) 1467-1472. https://doi.org/10.1111/j.1365-2621.2003.tb09668.x.
F. Chen, Y. Wei, B. Zhang, Characterization of water state and distribution in textured soybean protein using DSC and NMR, J. Food Eng. 100(3) (2010) 522-526. https://doi.org/10.1016/j.jfoodeng.2010.04.040.
Q. Zhou, P. Li, S. Fang, et al., Preservative effects of gelatin active coating containing eugenol and higher co2 concentration modified atmosphere packaging on chinese sea bass (Lateolabrax maculatus) during superchilling (-0.9 ℃) storage, Molecules 25(4) (2020) 871. https://doi.org/10.3390/molecules25040871.
S. Wang, J. Pang, P. Liang, Differential proteomics analysis of Penaeus vannamei muscles with quality characteristics by tmt quantitative proteomics during low-temperature storage, J. Agr. Food Chem. 69(10) (2021) 3247-3254. https://doi.org/10.1021/acs.jafc.0c08110.
L. Chen, H. Shi, Z. Li, et al., Molecular mechanism of protein dynamic change in Pacific oyster (Crassostrea gigas) during depuration at different salinities uncovered by mass spectrometry-based proteomics combined with bioinformatics, Food Chem. 394 (2022) 133454. https://doi.org/10.1016/j.foodchem.2022.133454.
J. Shi, L. Zhang, Y. Lei, et al., Differential proteomic analysis to identify proteins associated with quality traits of frozen mud shrimp (Solenocera melantho) using an iTRAQ-based strategy, Food Chem. 251 (2018) 25-32. https://doi.org/10.1016/j.foodchem.2018.01.046.
Y. Wang, J. Yan, Y. Ding, et al., Effects of ultrasound on the thawing of quick-frozen small yellow croaker (Larimichthys polyactis) based on TMTlabeled quantitative proteomic, Food Chem. 366 (2022) 130600. https://doi.org/10.1016/j.foodchem.2021.130600.
B. Zhang, C. Fang, G. Hao, et al., Effect of kappa-carrageenan oligosaccharides on myofibrillar protein oxidation in peeled shrimp (Litopenaeus vannamei) during long-term frozen storage, Food Chem. 245 (2018) 254-261. https://doi.org/10.1016/j.foodchem.2017.10.112.
P. Kittiphattanabawon, S. Benjakul, W. Visessanguan, et al., Cryoprotective effect of gelatin hydrolysate from blacktip shark skin on surimi subjected to different freeze-thaw cycles, LWT-Food Sci. Technol. 47(2) (2012) 437-442. https://doi.org/10.1016/j.lwt.2012.02.003.
M. Ohkubo, K. Osatomi, K. Hara, et al., Myofibrillar proteolysis by myofibril-bound serine protease from white croaker Argyrosomus argentatus, Fisheries Sci. 71(5) (2005) 1143-1148. https://doi.org/10.1111/j.1444-2906.2005.01074.x.
Y. Ge, Y. Li, T. Wu, et al., The preservation effect of CGA-Gel combined with partial freezing on sword prawn (Parapenaeopsis hardwickii), Food Chem. 313 (2020) 126078. https://doi.org/10.1016/j.foodchem.2019.126078.
S. Shui, H. Yao, Z. Jiang, et al., The differences of muscle proteins between neon flying squid (Ommastrephes bartramii) and jumbo squid (Dosidicus gigas) mantles via physicochemical and proteomic analyses, Food Chem. 364 (2021) 130374. https://doi.org/10.1016/j.foodchem.2021.130374.
N. Kimbuathong, P. Leelaphiwat, N. Harnkarnsujarit, Inhibition of melanosis and microbial growth in Pacific white shrimp (Litopenaeus vannamei) using high CO2 modified atmosphere packaging, Food Chem. 312 (2020) 126114. https://doi.org/10.1016/j.foodchem.2019.126114.
Y. Qian, J. Xie, S. Yang, et al., Effect of CO2 on chemical and microbial changes of pacific white shrimp during modified atmosphere packaging, J. Aquatic Food Product. Technol. 25(5) (2016) 644-655. https://doi.org/10.1080/10498850.2014.914117.
M. Zhang, F. Li, X. Diao, et al., Moisture migration, microstructure damage and protein structure changes in porcine longissimus muscle as influenced by multiple freeze-thaw cycles, Meat Sci. 133 (2017) 10-18. https://doi.org/10.1016/j.meatsci.2017.05.019.
D. Li, Y. Huang, K. Wang, et al., Microstructural characteristics of turbot (Scophthalmus maximus) muscle: effect of salting and processing, Int. J. Food Prop. 21(1) (2018) 1291-1302. https://doi.org/10.1080/10942912.2018.1460758.
X. Sun, L. Xiao, W. Lan, et al., Effects of temperature fluctuation on quality changes of large yellow croaker (Pseudosciaena crocea) with ice storage during logistics process, J. Food Process. Preserv. 42(2) (2018) e13505. https://doi.org/10.1111/jfpp.13505.
K. Okuda, A. Kawauchi, K. Yomogida, Quality improvements to mackerel (Scomber japonicus) muscle tissue frozen using a rapid freezer with the weak oscillating magnetic fields, Cryobiology 95 (2020) 130-137. https://doi.org/10.1016/j.cryobiol.2020.05.005.
L. Huang, S. Cheng, Y. Song, et al., Non-destructive analysis of caviar compositions using low-field nuclear magnetic resonance technique, J. Food Measurem. Character. 11(2) (2017) 621-628. https://doi.org/10.1007/s11694-016-9431-z.
Q. Zhou, P. Chu, C. Huang, et al., Ablation of Cypher, a PDZ-LIM domain Z-line protein, causes a severe form of congenital myopathy, J. Cell Biology. 155(4) (2001) 605-612. https://doi.org/10.1083/jcb.200107092.
M. Gallego, L. Mora, P. Fraser, et al., Degradation of LIM domain-binding protein three during processing of Spanish dry-cured ham, Food Chem. 149 (2014) 121-128. https://doi.org/10.1016/j.foodchem.2013.10.076.
R. Castellanos-Martínez, K. Jiménez-Camacho, M. Schnoor, et al., Cortactin expression in hematopoietic cells, The American J. Path. 190(5) (2020) 958-967. https://doi.org/10.1016/j.ajpath.2019.12.011.
M. Schnoor, T. E. Stradal, K.Rottner, Cortactin: cell functions of a multifaceted actin-binding protein, Trends Cell Biol. 28(2) (2018) 79-98. https://doi.org/10.1016/j.tcb.2017.10.009.
P. Tabatabaei-Panah, H. Moravvej, M. Alirajab, et al., COL17A1 gene polymorphisms are frequent in bullous pemphigoid, J. Eur. Acad. Dermatol. 35(8) (2021). https://doi.org/10.1111/jdv.17285.
C.W. Franzke, K. Tasanen, H. Schumann, et al., Collagenous transmembrane proteins: collagen XVⅡ as a prototype, Matrix Biol. 22(4) (2003) 299-309. https://doi.org/10.1016/S0945-053X(03)00051-9.
W. Li, X. Deng, J. Chen, RNA-binding proteins in regulating mRNA stability and translation: Roles and mechanisms in cancer, Semin. Cancer Biol. (2022) S1044579X22000827. https://doi.org/10.1016/j.semcancer.2022.03.025.
R. Kashikar, A.K. Kotha, S. Shah, et al., Advances in nanoparticle mediated targeting of RNA binding protein for cancer, Adv. Drug Deliver. Rev. 185 (2022) 114257. https://doi.org/10.1016/j.addr.2022.114257.
Q. Wang, J.L. Lin, S.Y. Chan, et al., The Xin repeat-containing protein, mXinβ, initiates the maturation of the intercalated discs during postnatal heart development, Dev. Biol. 374(2) (2013) 264-280. https://doi.org/10.1016/j.ydbio.2012.12.007.
P. Zobaroğlu Özer, D. Koyunoğlu, Ç.D. Son, et al., SMN loss dysregulates microtubule-associated proteins in spinal muscular atrophy model, Mol. Cell. Neurosci. 120 (2022) 103725. https://doi.org/10.1016/j.mcn.2022.103725.
S. Bodakuntla, A.S. Jijumon, C. Villablanca, et al., Microtubule-associated proteins: structuring the cytoskeleton, Trends Cell Biol. 29(10) (2019) 804-819. https://doi.org/10.1016/j.tcb.2019.07.004.
S. Khwaja, K. Kumar, R. Das, et al., Microtubule associated proteins as targets for anticancer drug development, Bioorg. Chem. 116 (2021) 105320. https://doi.org/10.1016/j.bioorg.2021.105320.
K.L. Moynihan, R. Pooley, P.M. Miller, et al., Murine CENP-F regulates centrosomal microtubule nucleation and interacts with Hook2 at the centrosome, Mol. Biol. Cell 20(22) (2009) 4790-4803. https://doi.org/10.1091/mbc.e09-07-0560.
G. Szebenyi, W.C. Wigley, B. Hall, et al., Hook2 contributes to aggresome formation, BMC Cell Biol. 8(1) (2007) 19. https://doi.org/10.1186/1471-2121-8-19.
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