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Effect of Carboxymethyl Chitosan Magnetic Nanoparticles Plus Herring Antifreeze Protein on Conformation and Oxidation of Myofibrillar Protein From Red Sea Bream (Pagrosomus major) After Freeze-Thaw Treatment

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Abstract

The effects on the quality of frozen red sea bream, which were pretreated by soaking in solutions containing trehalose, carboxymethyl chitosan magnetic nanoparticles (CCMN), and glycerin or 0.1% herring antifreeze protein (hAFP), were investigated. In this study, the viscoelastic properties of protein studied with the dynamic rheology, Raman and intrinsic fluorescence spectrometry were used to explore the conformation changes of MFP. Surface hydrophobicity, particle size, and zeta potential were carried out to analyze protein aggregation. Solubility, the content of total sulfhydryl/disulfide bond/carbonyl/dityrosine, and the Ca2+-ATPase activity were measured to explore the degree of protein oxidation. SDS-PAGE was conducted to analyze the protein denaturation. Results showed that the pretreatment of red sea bream with soak solutions could improve the viscoelasticity of fillets protein, stabilize the secondary and tertiary conformation of the MFP, inhibit the protein aggregation and oxidation, and decrease the degree of protein denaturation compared with the control (4 °C thawing), especially the soak solutions containing hAFP could minimize the freeze-thaw damage. To summarize, the hAFP helped to retain the above characteristics of frozen fillets much better than that of conventional cryoprotectants (glycerin) to improve the quality of the frozen product after thawing.

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References

  • Bar, D. M., Braslavsky, I., & Davies, P. L. (2016). Ice-binding proteins and their function. Annual Review of Biochemistry, 85, 515–542.

    Google Scholar 

  • Beliciu, C. M., & Moraru, C. I. (2011). The effect of protein concentration and heat treatment temperature on micellar casein-soy protein mixtures. Food Hydrocolloids, 25(6), 1448–1460.

    CAS  Google Scholar 

  • Boonsupthip, W., & Lee, T. C. (2010). Application of antifreeze protein for food preservation: effect of type III antifreeze protein for preservation of gel-forming of frozen and chilled actomyosin. Journal of Food Science, 68(5), 1804–1809.

    Google Scholar 

  • Carew, E. B., Asher, I. M., & Stanley, H. E. (1975). Laser Raman spectroscopy--new probe of myosin substructure. Science, 188(4191), 933–936.

    CAS  PubMed  Google Scholar 

  • Campo-Deaño, L., Tovar, C. A., Pombo, M. J., Solas, M. T., & Borderías, A. J. (2009). Rheological study of giant squid surimi (Dosidicus gigas) made by two methods with different cryoprotectants added. Journal of Food Engineering, 94(1), 26–33.

    Google Scholar 

  • Cao, M. J., Cao, A. L., Wang, J., Cai, L. Y., Regenstein, J., Ruan, Y. J., & Li, X. X. (2018). Effect of magnetic nanoparticles plus microwave or far-infrared thawing on protein conformation changes and moisture migration of red sea bream (Pagrus major) fillets. Food Chemistry, 266, 498–507.

    CAS  PubMed  Google Scholar 

  • Cao, Y., & Xiong, Y. L. (2015). Chlorogenic acid-mediated gel formation of oxidatively stressed MP. Food Chemistry, 180, 235–243.

    CAS  PubMed  Google Scholar 

  • Cai, L., Cao, M., Cao, A., Regenstein, J., Li, J., & Guan, R. (2018). Ultrasound or microwave vacuum thawing of red sea bream (Pagrus major) fillets. Ultrasonics Sonochemistry, 47, 122–132.

    CAS  PubMed  Google Scholar 

  • Colombo, G., Clerici, M., Giustarini, D., Portinaro, N., Badalamenti, S., Rossi, R., et al. (2015). A central role for intermolecular dityrosine cross-linking of fibrinogen in high molecular weight advanced oxidation protein product (aopp) formation. Biochim Biophys Acta, 1850(1), 1–12.

    CAS  PubMed  Google Scholar 

  • Cosminm, B., & Carmeni, M. (2011). The effect of protein concentration and heat treatment temperature on micellar casein-soy protein mixtures. Food Hydrocolloids, 25(6), 1448–1460.

    Google Scholar 

  • Cruz, R. M. S., Vieira, M. C., & Silva, C. L. M. (2009). The response of watercress (Nasturtium officinale) to vacuum impregnation: Effect of an antifreeze protein type I. Journal of Food Engineering, 95(2), 339–345.

    Google Scholar 

  • Davies, P. L. (2014). Ice-binding proteins: a remarkable diversity of structures for stopping and starting ice growth. Trends in Biochemical Sciences, 39(11), 548–555.

    CAS  PubMed  Google Scholar 

  • Davies, K. J. A., Delsignore, M. E., & Lin, S. W. (1987). Protein damage and degradation by oxygen radicals. ii. modification of amino acids. Journal of Biological Chemistry, 262(20), 9902–9907.

    CAS  PubMed  Google Scholar 

  • Ding, X., Zhang, H., Wang, L., Qian, H., Qi, X., & Xiao, J. (2015). Effect of barley antifreeze protein on thermal properties and water state of dough during freezing and freeze-thaw cycles. Food Hydrocolloids, 47, 32–40.

    CAS  Google Scholar 

  • Evans, R. P., & Fletcher, G. L. (2010). Type I antifreeze proteins expressed in snailfish skin are identical to their plasma counterparts. Febs Journal, 272(20), 5327–5336.

    Google Scholar 

  • Faraji, M., Yamini, Y., & Rezaee, M. (2010). Magnetic nanoparticles: synthesis, stabilization, functionalization, characterization, and applications. Journal of the Iranian Chemical Society, 7(1), 1–37.

    CAS  Google Scholar 

  • Gómez-Estaca, J., Montero, P., & Gómez-Guillén, M. C. (2014). Shrimp (Litopenaeus vannamei) muscle proteins as source to develop edible films. Food Hydrocolloids, 41(41), 86–94.

    Google Scholar 

  • Gonçalves, A. A. (2009). Ozone - an emerging technology for the seafood industry. Brazilian Archives of Biology & Technology, 52(6), 1527–1539.

    Google Scholar 

  • Gornall, A. G., Bardawill, C. J., & David, M. M. (1949). Determination of serum proteins by means of biuret reaction. Journal of biological chemistry, 177(2), 751–766.

    CAS  PubMed  Google Scholar 

  • Herrero, A. M. (2008). Raman spectroscopy for monitoring protein structure in muscle food systems. Critical Reviews in Food Science & Nutrition, 48(6), 512–523.

    CAS  Google Scholar 

  • Jantakoson, T., Thavaroj, W., & Konno, K. (2013). Myosin and actin denaturation in frozen stored kuruma prawn Marsupenaeus japonicus myofibrils. Fisheries Science, 79(2), 341–347.

    CAS  Google Scholar 

  • Ko, W. C., Shi, H. Z., Chang, C. K., Huang, Y. H., Chen, Y. A., & Hsieh, C. W. (2016). Effect of adjustable parallel high voltage on biochemical indicators and actomyosin Ca2+-ATPase from tilapia (Oreochromis niloticus). LWT - Food Science and Technology, 69, 417–423.

    CAS  Google Scholar 

  • Koch, L., Emin, M. A., & Schuchmann, H. P. (2017). Reaction behaviour of highly concentrated whey protein isolate under defined heat treatments. International Dairy Journal, 71, 114–121.

    CAS  Google Scholar 

  • Kong, C. H. Z., Hamid, N., Liu, T., & Sarojini, V. (2016). Effect of antifreeze peptide pretreatment on ice crystal size, drip loss, texture, and volatile compounds of frozen carrots. Journal of Agricultural & Food Chemistry, 64(21), 4327–4336.

    CAS  Google Scholar 

  • Kong, C. H. Z., Hamid, N., Ma, Q., Lu, J., Wang, B. G., & Sarojini, V. (2017). Antifreeze peptide pretreatment minimizes freeze-thaw damage to cherries: an in-depth investigation. LWT - Food Science and Technology, 84, 1–29.

    Google Scholar 

  • Langevin, D. (2014). Surface shear rheology of monolayers at the surface of water. Advances in Colloid & Interface Science, 207(1), 121–130.

    CAS  Google Scholar 

  • Liang, Y. Y., & Zhang, L. M. (2007). Bioconjugation of papain on superparamagnetic nanoparticles decorated with carboxymethylated chitosan. Biomacromolecules, 8(5), 1480–1486.

    CAS  PubMed  Google Scholar 

  • Liu, Q., Lu, Y., Han, J. C., Chen, Q., & Kong, B. H. (2015). Structure-modification by moderate oxidation in hydroxyl radical-generating systems promote the emulsifying properties of soy protein isolate. Food Structure, 6, 21–28.

    Google Scholar 

  • Lu, H., Zhang, L. T., Li, Q. Z., & Luo, Y. K. (2017). Comparison of gel properties and biochemical characteristics of myofibrillar protein from bighead carp (Aristichthys nobilis) affected by frozen storage and a hydroxyl radical-generation oxidizing system. Food Chemistry, 223, 96–103.

    CAS  PubMed  Google Scholar 

  • Lv, M., Mei, K., Zhang, H., Xu, D., & Yang, W. (2018). Effects of electron beam irradiation on the biochemical properties and structure of myofibrillar protein from Tegillarca granosa, meat. Food Chemistry, 254, 64–69.

    CAS  PubMed  Google Scholar 

  • Manuchehrabadi, N., Zhe, G., Zhang, J. J., Ring, H. L., Shao, Q., Liu, F., McDermott, M., Fok, A., Rabin, Y., Brockbank, K. G. M., Garwood, M., Haynes, C. L., & Bischof, J. C. (2017). Improved tissue cryopreservation using inductive heating of magnetic nanoparticles [J]. Science Translational Medicine, 9(379), eaah4586–eaah4597.

    PubMed  PubMed Central  Google Scholar 

  • Hernández-Martínez, M., Gallardo-Velázquez, T., Osorio-Revilla, G., Almaraz-Abarca, N., & Castañeda-Pérez, E. (2014). Application of MIR-FTIR spectroscopy and chemometrics to the rapid prediction of fish fillet quality. CyTA - Journal of Food, 12(4), 369–377.

    Google Scholar 

  • Mao, W. J., Li, X. L., Fukuoka, M., Liu, S. C., Ji, H. W., & Sakai, N. (2016). Study of Ca2+-ATPase activity and solubility in the whole kuruma prawn (Marsupenaeus japonicus) meat during heating: based on the kinetics analysis of myofibril protein thermal denaturation. Food and Bioprocess Technology, 9(9), 1511–1520.

    CAS  Google Scholar 

  • Mehta, N. K., & Nayak, B. B. (2017). Bio-chemical composition, functional and rheological properties of fresh meat from fish, squid and shrimp: a comparative study. International Journal of Food Properties.

  • Nielsen, M. K., & Jørgensen, B. M. (2004). Quantitative relationship between trimethylamine oxide aldolase activity and formaldehyde accumulation in white muscle from gadiform fish during frozen storage. Journal of Agricultural & Food Chemistry, 52(12), 3814–3822

  • Ohta, F., & Yamada, T. (2011). On the correlation between the concentrations of phosphates and chlorides in the unfrozen portions of the frozen fish muscle juices and the denaturation rate of fish muscle protein during frozen-storage. Transactions of the Japan Society of Refrigerating & Air Conditioning Engineers, 7(09), 1893–1898.

    Google Scholar 

  • Peng, B., Li, Y. Q., Ding, S. Y., & Yang, J. (2017). Characterization of textural, rheological, thermal, microstructural, and water mobility in wheat flour dough and bread affected by trehalose. Food Chemistry, 233, 369–377.

    CAS  PubMed  Google Scholar 

  • Shi, Y., Li, R. Y., Tu, Z. C., Ma, D., Wang, H., & Huang, X. Q. (2015). Effect of γ-irradiation on the physicochemical properties and structure of fish myofibrillar proteins. Radiation Physics and Chemistry, 109(10), 70–72.

    CAS  Google Scholar 

  • Sun, W. Z., Zhao, Q. Z., Zhao, M. M., Yang, B., Cui, C., & Ren, J. Y. (2011). Structural evaluation of myofibrillar proteins during processing of Cantonese sausage by Raman spectroscopy. Journal of Agricultural & Food Chemistry, 59(20), 11070–11077.

    CAS  Google Scholar 

  • Sun, X. D., & Arntfield, S. D. (2012). Gelation properties of chicken myofibrillar protein induced by transglutaminase crosslinking. Journal of Food Engineering, 107(2), 226–233.

    Google Scholar 

  • Wong, B. T., Li, D., & Augustin, M. A. (2011). Deamidated wheat protein-dextran Maillard conjugates: effect of size and location of polysaccharide conjugated on steric stabilization of emulsions at acidic pH. Food Hydrocolloids, 25(6), 1424–1432.

    CAS  Google Scholar 

  • Xia, X., Kong, B., Liu, Q., & Liu, J. (2009). Physicochemical change and protein oxidation in porcine longissimus dorsi as influenced by different freeze-thaw cycles. Meat Science, 83(2), 239–245.

    CAS  PubMed  Google Scholar 

  • Xiong, G., Han, M., Kang, Z., Zhao, Y., Xu, X., & Zhu, Y. (2016). Evaluation of protein structural changes and water mobility in chicken liver paste batters prepared with plant oil substituting pork back-fat combined with pre-emulsification. Food Chemistry, 196, 388–395.

    CAS  PubMed  Google Scholar 

  • Yeh, C. M., Kao, B. Y., & Peng, H. J. (2009). Production of a recombinant type 1 antifreeze protein analogue by L. lactis and its applications on frozen meat and frozen dough. Journal of Agricultural & Food Chemistry, 57(14), 6216–6223.

    CAS  Google Scholar 

  • Zhang, T., Li, Z. J., Wang, Y. M., Xue, Y., & Xue, C. H. (2016). Effects of konjac glucomannan on heat-induced changes of physicochemical and structural properties of surimi gels. Food Research International, 83, 152–161.

    CAS  Google Scholar 

  • Zhang, T., Xue, Y., Li, Z., Wang, Y., Yang, W., & Xue, C. (2015). Effects of ozone-induced oxidation on the physicochemical properties of myofibrillar proteins recovered from bighead carp (Hypophthalmichthys nobilis). Food and Bioprocess Technology, 8(1), 181–190.

    CAS  Google Scholar 

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Funding

This study was supported by the National Key R&D Program of China (2018YFD0901106), the Science and Technology Project by General Administration of Quality Supervision, Inspection and Quarantine of China (2017IK090), the National Natural Science Foundation of China (31401478), the Natural Science Foundation of Liaoning Province of China (20170540006), and the Aquatic Products Processing and Safety Key Laboratory of Guangdong Province (GDPKLAPPS1805).

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Authors and Affiliations

  1. Ningbo Research Institute, Zhejiang University, Ningbo, 315100, China

    Luyun Cai

  2. College of Biosystems Engineering and Food Science, National & Local Joint Engineering Laboratory of Intelligent Food Technology and Equipment, Zhejiang University, Hangzhou, 310058, China

    Luyun Cai

  3. Department of Food Quality and Safety/National R&D Center for Chinese Herbal Medicine Processing, College of Engineering, China Pharmaceutical University, Nanjing, 211198, China

    Linyu Nian

  4. National & Local Joint Engineering Research Center of Storage, Processing and Safety Control Technology for Fresh Agricultural and Aquatic Products, College of Food Science and Engineering, Bohai University, Jinzhou, 121013, China

    Linyu Nian & Xiuxia Li

  5. Hangzhou Customs District, Hangzhou, 310007, China

    Ailing Cao

  6. College of Food Science, Southwest University, Chongqing, 400715, China

    Yuhao Zhang

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  1. Luyun Cai
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Cai, L., Nian, L., Cao, A. et al. Effect of Carboxymethyl Chitosan Magnetic Nanoparticles Plus Herring Antifreeze Protein on Conformation and Oxidation of Myofibrillar Protein From Red Sea Bream (Pagrosomus major) After Freeze-Thaw Treatment. Food Bioprocess Technol 13, 355–366 (2020). https://doi.org/10.1007/s11947-019-02384-x

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