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This study focused on the effect of tea polyphenols on the quality changes of low-salt grass carp cured products during refrigeration. The addition of tea polyphenols could be found to improve the color and texture of the cured grass carp products during the refrigeration process. The bacterial colonies (TVC) and total volatile basic nitrogen (TVB-N) content showed that the conditioned grass carp fillets had a high level of food safety. The thiobarbituric acid reactive substance (TBARs) value of grass carp continued to rise with increasing refrigeration time, indicating that fat oxidation occurred in the grass carp cured products. The addition of tea polyphenols was found to inhibit protein oxidation and protect the protein structure of the low-salt conditioned grass carp fillets during refrigeration, as indicated by the indicators related to protein oxidation. This finding provides a new theoretical idea for grass carp processing and storage.


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Analysis of changes in low-salt conditioned grass carp (Ctenopharyngodon idella) fillets during refrigeration in terms of quality and protein stability

Show Author's information Jingqi Xue1Dajun Wang2Shumin Zhang2Lunan Jing1Hao Pan1Wenzheng Shi1( )
College of Food Science and Technology, Shanghai Ocean University, Shanghai 201306, China
Yantai Haiyu Foodstuffs Co., Ltd. (Yantai), Yantai 264000, China

Abstract

This study focused on the effect of tea polyphenols on the quality changes of low-salt grass carp cured products during refrigeration. The addition of tea polyphenols could be found to improve the color and texture of the cured grass carp products during the refrigeration process. The bacterial colonies (TVC) and total volatile basic nitrogen (TVB-N) content showed that the conditioned grass carp fillets had a high level of food safety. The thiobarbituric acid reactive substance (TBARs) value of grass carp continued to rise with increasing refrigeration time, indicating that fat oxidation occurred in the grass carp cured products. The addition of tea polyphenols was found to inhibit protein oxidation and protect the protein structure of the low-salt conditioned grass carp fillets during refrigeration, as indicated by the indicators related to protein oxidation. This finding provides a new theoretical idea for grass carp processing and storage.

Keywords: tea polyphenols, protein oxidation, grass carp, pickling, low-salt

References(41)

[1]
FAO. The state of world fisheries and aquaculture 2022: Torwards blue transformation. Rome: Food and Agriculture Organization.
[2]

Y. Zhang, W. T. Liu, G. Y. Li, et al., Isolation and partial characterization of pepsin-soluble collagen from the skin of grass carp (Ctenopharyngodon idella), Food Chem. 103 (2007) 906–912. https://doi.org/10.1016/j.foodchem.2006.09.053.

[3]

J. B. Zhang, Y. Liu, X. C. Liu, et al., Characterization of the microbial composition and quality of lightly salted grass crap (Ctenopharyngodon idella) fillets with vacuum or modified atmosphere packaging, Int. J. Food Microbiol. 293 (2019) 87–93. https://doi.org/10.1016/j.ijfoodmicro.2018.12.022.

[4]
I. V. Andreetta-Gorelkina, I. V. Gorelkin, T. Rustad. Determination of apparent diffusion coefficient in balls made from haddock mince during brining, J. Food Eng. 175 (2016) 8–14. https://doi.org/10.1016/j.jfoodeng.2015.11.016.
DOI
[5]

Q. Q. Jiang, Y. F. Du, S. Y. Huang, et al., Physicochemical and microstructural mechanisms for quality changes of lightly salted tilapia (Oreochromis niloticus) fillets during frozen storage, J. Sci. Food Agr. 103 (2022) 308–316. https://doi.org/10.1002/jsfa.12142.

[6]

T. Zhou, Y. X. Ding, S. Benjakul, et al., Characterization of endogenous enzymes in sword prawn (Parapenaeopsis hardwickii) and their effects on the quality of muscle proteins during frozen storage, LWT-Food Sci Technol. 177 (2023) 114563. https://doi.org/10.1016/j.lwt.2023.114563.

[7]

X. B. Nie, L. H. Wang, Q. Wang, et al., Effect of a sodium alginate coating infused with tea polyphenols on the quality of fresh Japanese sea bass (Lateolabrax japonicas) fillets, J. Food Sci. 83 (2018) 1695–1700. https://doi.org/10.1111/1750-3841.14184.

[8]

H. K. Xie, D. Y. Zhou, Z. Y. Zhou, et al., Effects of natural phenolics on shelf life and lipid stability of freeze-dried scallop adductor muscle, Food Chem. 295 (2019) 423–431. https://doi.org/10.1016/j.foodchem.2019.05.133.

[9]

X. X. Zhou, T. Chen, H. H. Lin, et al., Physicochemical properties and microstructure of surimi treated with egg white modified by tea polyphenols, Food Hydrocoll. 90 (2019) 82–89. https://doi.org/10.1016/j.foodhyd.2018.07.031.

[10]

Q. Q. Jiang, R. Jia, N. Nakazawa, et al., Changes in protein properties and tissue histology of tuna meat as affected by salting and subsequent freezing, Food Chem. 271 (2019) 550–560. https://doi.org/10.1016/j.foodchem.2018.07.219.

[11]

T. T. Li, W. Z. Hu, J. R. Li, et al., Coating effects of tea polyphenol and rosemary extract combined with chitosan on the storage quality of large yellow croaker (Pseudosciaena crocea), Food Control 25 (2012) 101–106. https://doi.org/10.1016/j.foodcont.2011.10.029.

[12]

X. P. Li, J. R. Li, J. L. Zhu, et al., Postmortem changes in yellow grouper (Epinephelus awoara) fillets stored under vacuum packaging at 0 ℃, Food Chem. 126 (2011) 896–901. https://doi.org/10.1016/j.foodchem.2010.11.071.

[13]

Y. X. Wang, H. Y. Huang, W. Z. Shi, Effect of different drying time on physicochemical properties of black carp (Mylopharyngodon piceus) by hot air, J. Food Process Pres. 46 (2021) 16217. https://doi.org/10.1111/jfpp.16217.

[14]

J. Fernández, J. A. Pérez-Álvarez, J. A. Fernández-López, Thiobarbituric acid test for monitoring lipid oxidation in meat, Food Chem. 59 (1997) 345–353. https://doi.org/10.1016/S0308-8146(96)00114-8.

[15]
Z. Teymouri, H. Shekarchizadeh. A colorimetric indicator based on copper nanoparticles for volatile sulfur compounds to monitor fish spoilage in intelligent packaging, Food Packaging Shelf. 33 (2022) 100884. https://doi.org/10.1016/j.fpsl.2022.100884.
DOI
[16]

H. Mu, L. Li, C. B. Yang, et al., Effects of dietary fishmeal levels on adenosine triphosphate-related compounds and freshness of raw and cooked muscle in large yellow croaker, Aquac. Rep. 26 (2022) 101304. https://doi.org/10.1016/j.aqrep.2022.101304.

[17]

L. Kong, C. F. Cai, Y. T. Ye, et al., Comparison of non-volatile compounds and sensory characteristics of Chinese mitten crabs (Eriocheir sinensis) reared in lakes and ponds: potential environmental factors, Aquaculture 364/365 (2012) 96–102. https://doi.org/10.1016/j.aquaculture.2012.08.008.

[18]

X. F. Liu, X. J. Sun, Y. J. Wei, et al., Effects of ultrasonic treatment on physico-chemical properties and structure of tuna (Thunnus tonggol) myofibrillar proteins, J. Food Compos. Anal. 108 (2022) 104438. https://doi.org/10.1016/j.jfca.2022.104438.

[19]

D. Zhang, Z. C. Wu, J. G. Ruan, et al., Effects of lysine and arginine addition combined with high-pressure microfluidization treatment on the structure, solubility, and stability of pork myofibrillar proteins, LWT-Food Sci. Technol. 172 (2022) 114190. https://doi.org/10.1016/j.lwt.2022.114190.

[20]

S. Phatcharat, S. Benjakul, W. Visessanguan, et al., Effects of washing with oxidising agents on the gel-forming ability and physicochemical properties of surimi produced from bigeye snapper (Priacanthus tayenus), Food Chem. 98 (2006) 431–439. https://doi.org/10.1016/j.foodchem.2005.06.016.

[21]

J. Yongsawatdigul, J. W. Park, Thermal denaturation and aggregation of threadfin bream actomyosin, Food Chem. 83 (2003) 409–416. https://doi.org/10.1016/S0308-8146(03)00105-5.

[22]
I. Chelh, P. Gatellier, V. Santé-Lhoutellier. Technical note: a simplified procedure for myofibril hydrophobicity determination, Meat Sci. 74 (2006) 681–683. https://doi.org/10.1016/j.meatsci.2006.05.019.
DOI
[23]

H. Xiao, J. Yu, L. L. Song, et al., Characterization of flesh firmness and ease of separation in the fermentation of sea bass in terms of protein structure, texture, and muscle tissue structural changes, Food Res. Int. 162 (2022) 111965. https://doi.org/10.1016/j.foodres.2022.111965.

[24]

D. W. Kong, R. W. Han, M. D. Yuan, et al., Ultrasound combined with slightly acidic electrolyzed water thawing of mutton: effects on physicochemical properties, oxidation and structure of myofibrillar protein, Ultrason. Sonochem. 93 (2023) 106309. https://doi.org/10.1016/j.ultsonch.2023.106309.

[25]

N. Qin, L. Zhang, J. Zhang, et al., Influence of lightly salting and sugaring on the quality and water distribution of grass carp (Ctenopharyngodon idella) during super-chilled storage, J. Food Eng. 215 (2017) 104–112. https://doi.org/10.1016/j.jfoodeng.2017.07.011.

[26]

R. Wang, X. Hu, A. K. Agyekumwaa, et al., Synergistic effect of kojic acid and tea polyphenols on bacterial inhibition and quality maintenance of refrigerated sea bass (Lateolabrax japonicus) fillets, LWT-Food Sci. Technol. 137 (2021) 110452. https://doi.org/10.1016/j.lwt.2020.110452.

[27]

H. M. M. Hernández, G. Duflos, P. Malle, et al., Collagenase activity and protein hydrolysis as related to spoilage of iced cod (Gadus morhua), Food Res. Int. 36 (2003) 141–147. https://doi.org/10.1016/S0963-9969(02)00129-1.

[28]

F. Shahidi, P. Ambigaipalan, Phenolics and polyphenolics in foods, beverages and spices: antioxidant activity and health effects: a review, J. Funct. Foods 18 (2015) 820–897. https://doi.org/10.1016/j.jff.2015.06.018.

[29]

W. J. Fan, Y. L. Chi, S. Zhang, The uses of a tea polyphenol dip to extend the shelf life of silver carp (Hypophthalmicthys molitrix) during storage in ice, Food Chem. 108 (2008) 148–153. https://doi.org/10.1016/j.foodchem.2007.10.057.

[30]

W. Khalid, M. S. Arshad, M. Yasin, et al., Quality characteristics of gamma irradiation and kale leaf powder treated ostrich and chicken meat during storage, Int. J. Food Prop. 24 (2021) 1335–1348. https://doi.org/10.1080/10942912.2021.1963274.

[31]

Z. Q. Pan, L. Lin, Z. H. Shen, et al., Effects of tea polyphenol treatments on the quality and microbiota of crisp grass carp fillets during storage at 4 ℃, Appl. Sci. 11 (2021) 4370. https://doi.org/10.3390/app11104370.

[32]

M. D. Navarro-Martinez, E. Navarro-Peran, J. Cabezas-Herrera, et al., Antifolate activity of epigallocatechin gallate against Stenotrophomonas maltophilia, Antimicrob. Agents Chem. 49 (2005) 2914–2920. https://doi.org/10.1128/aac.49.7.2914-2920.2005.

[33]
T. Saito, K. Arai, M. Matsuyoshi, et al., A new method for estimating the freshness of fish, Bulletin of the Japanese Society of Scientific Fisheries, 1959.
DOI
[34]

A. Amiri, P. Sharifian, N. Morakabati, et al., Modification of functional, rheological and structural characteristics of myofibrillar proteins by high-intensity ultrasonic and papain treatment, Innov. Food Sci. Emerg. Technol. 72 (2021) 102748. https://doi.org/10.1016/j.ifset.2021.102748.

[35]

W. Wan, J. Feng, H. Wang, et al., Influence of repeated freeze-thaw treatments on the oxidation and degradation of muscle proteins from mirror carp (Cyprinus carpio L.), based on myofibrillar protein structural changes, Int. J. Biol. Macromol. 226 (2023) 454–462. https://doi.org/10.1016/j.ijbiomac.2022.12.082.

[36]

S. X. Wang, Y. M. Zhang, L. Chen, et al., Dose-dependent effects of rosmarinic acid on formation of oxidatively stressed myofibrillar protein emulsion gel at different NaCl concentrations, Food Chem. 243 (2018) 50–57. https://doi.org/10.1016/j.foodchem.2017.09.114.

[37]

C. Zhang, Y. X. Li, X. F. Xia, et al., Changes in protein oxidation, structure, and thermal stability of chicken breast subjected to ultrasound-assisted immersion freezing during frozen storage, Food Chem. 398 (2023) 133874. https://doi.org/10.1016/j.foodchem.2022.133874.

[38]

X. Li, J. Y. Wang, X. Q. Gao, et al., Inhibitory effects of lotus seedpod procyanidins against lipid and protein oxidation and spoilage organisms in chilled-storage beef, LWT-Food Sci. Technol. 160 (2022) 113247. https://doi.org/10.1016/j.lwt.2022.113247.

[39]

J. X. Pei, J. Mei, G. Wu, et al., Gum tragacanth-sodium alginate active coatings containing epigallocatechin gallate reduce hydrogen peroxide content and inhibit lipid and protein oxidations of large yellow croaker (Larimichthys crocea) during super-chilling storage, Food Chem. 397 (2022) 133792. https://doi.org/10.1016/j.foodchem.2022.133792.

[40]

C. Q. Li, Y. L. Xiong, J. Chen, et al., Oxidation-induced unfolding facilitates myosin cross-linking in myofibrillar protein by microbial transglutaminase, J. Agr. Food Chem. 60 (2012) 8020–8027. https://doi.org/10.1021/jf302150h.

[41]

J. Kroll, H. M. Rawel, S. Rohn, Reactions of plant phenolics with food proteins and enzymes under special consideration of covalent bonds, Food Sci. Technol. Res. 9 (2003) 205–218. https://doi.org/10.3136/fstr.9.205.

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Publication history

Received: 24 July 2023
Revised: 21 August 2023
Accepted: 24 August 2023
Published: 16 November 2023
Issue date: October 2023

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© Beijing Academy of Food Sciences 2023.

Acknowledgements

This work was supported by the National Key R&D Program of China (2022YFD2100902) and the Yantai Science and Technology Innovation Development Plan Project (2022YT0620061).

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Food Science of Animal Products published by Tsinghua University Press. This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).

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