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The protective effect of ice glazing with 1.5% chitosan (CH) during the freeze-thaw (F-T) cycles on the quality and myofibrillar protein (MP) structure of fish balls was investigated. The results showed that the F-T cycles led to a significant increase in the amount of frost generation (from 0.34% to 13.57%) and ice crystal diameter (from 15.78 to 37.83 μm) on the surface of frozen fish balls. In addition, the quality of fish ball was significantly decreased and the structure of MP was damaged during F-T cycles (P < 0.05). Ice-glazing with CH decreased the thawing loss, cooking loss, and centrifugal loss of fish balls by 36.10%, 33.18%, and 32.11%, respectively, compared to control group. Moreover, ice-glazing with CH can maintain the MP structure of fish balls during F-T cycles. Compared with the control group, the surface hydrophobicity of CH ice-glazed samples was reduced by 35.78%, the content of free amino acids was increased by 24.86%. It can be concluded that ice glazing with CH is effective to inhibit the deterioration of quality and MP structure of fish balls.


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Effect of ice glazing with chitosan on the quality and myofibrillar protein structure of fish balls induced by freeze-thaw cycles

Show Author's information Xiaoxiang Yue1,2Fang Zhou3Nan Pan2Yihong Bao1Fangfei Li1( )Xiufang Xia2( )
College of Life Science, Northeast Forestry University, Harbin 150040, China
College of Food Science, Northeast Agricultural University, Harbin 150030, China
The Academy of Quality Inspection and Research in Heilongjiang Province, Harbin 150020, China

Abstract

The protective effect of ice glazing with 1.5% chitosan (CH) during the freeze-thaw (F-T) cycles on the quality and myofibrillar protein (MP) structure of fish balls was investigated. The results showed that the F-T cycles led to a significant increase in the amount of frost generation (from 0.34% to 13.57%) and ice crystal diameter (from 15.78 to 37.83 μm) on the surface of frozen fish balls. In addition, the quality of fish ball was significantly decreased and the structure of MP was damaged during F-T cycles (P < 0.05). Ice-glazing with CH decreased the thawing loss, cooking loss, and centrifugal loss of fish balls by 36.10%, 33.18%, and 32.11%, respectively, compared to control group. Moreover, ice-glazing with CH can maintain the MP structure of fish balls during F-T cycles. Compared with the control group, the surface hydrophobicity of CH ice-glazed samples was reduced by 35.78%, the content of free amino acids was increased by 24.86%. It can be concluded that ice glazing with CH is effective to inhibit the deterioration of quality and MP structure of fish balls.

Keywords: Chitosan, Quality, Myofibrillar protein, Fish balls, Ice glazing

References(42)

[1]

X. Du, H. J. Li, C. H. Dong, et al., Effect of ice structuring protein on the microstructure and myofibrillar protein structure of mirror carp (Cyprinus carpio L.) induced by freeze-thaw processes, LWT-Food Sci. Technol. 139 (2021) 110570. https://doi.org/10.1016/j.lwt.2020.110570.

[2]

L. Fan, D. Ruan, J. Shen, et al., The role of water and oil migration in juiciness loss of stuffed fish ball with the fillings of pig fat/meat as affected by freeze-thaw cycles and cooking process, LWT-Food Sci. Technol. 159 (2022) 113244. https://doi.org/10.1016/j.lwt.2022.113244.

[3]
B. Wang, F. F. Li, N. Pan, et al., Effect of ice structuring protein on the quality of quick-frozen patties subjected to multiple freeze-thaw cycles, Meat Sci. 172 (2021) 108335. https://doi.org/10.1016/j.meatsci.2020.108335.
DOI
[4]

N. Pan, C. H. Dong, X. Du, et al., Effect of freeze-thaw cycles on the quality of quick-frozen pork patty with different fat content by consumer assessment and instrument-based detection, Meat Sci. 172 (2020) 108313. https://doi.org/10.1016/j.meatsci.2020.108313.

[5]

F. F. Li, X. Du, Y. M. Ren, et al., Impact of ice structuring protein on myofibrillar protein aggregation behaviour and structural property of quick-frozen patty during frozen storage, Int. J. Biol. Macromol. 178 (2021) 136–142. https://doi.org/10.1016/j.ijbiomac.2021.02.158.

[6]

R. Li, M. Guo, E. Liao, et al., Effects of repeated freezing and thawing on myofibrillar protein and quality characteristics of marinated Enshi black pork, Food Chem. 378 (2022) 131994. https://doi.org/10.1016/j.foodchem.2021.131994.

[7]

F. F. Li, B. Wang, B. H. Kong, et al., Decreased gelling properties of protein in mirror carp (Cyprinus carpio) are due to protein aggregation and structure deterioration when subjected to freeze-thaw cycles, Food Hydrocoll. 97 (2019) 105223. https://doi.org/10.1016/j.foodhyd.2019.105223.

[8]

M. C. Zhang, F. F. Li, X. Q. 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.

[9]

M. C. Zhang, H. L. Niu, Q. Chen, et al., Influence of ultrasound-assisted immersion freezing on the freezing rate and quality of porcine Longissimus muscles, Meat Sci. 136 (2018) 1–8. https://doi.org/10.1016/j.meatsci.2017.10.005.

[10]

D. van der Sman, Clumping of frozen par-fried foods: lessons from frosting on structured surfaces, Food Str. 17 (2018) 9–20. https://doi.org/10.1016/j.foostr.2018.06.001.

[11]

O. Laguerre, D. Flick, Frost formation on frozen products preserved in domestic freezers, J. Food. Eng. 79(1) (2007) 124–136. https://doi.org/10.1016/j.jfoodeng.2006.01.036.

[12]

S. Herianto, M. K. Shih, C. M. Lin, et al., The effects of glazing with plasma-activated water generated by a piezoelectric direct discharge plasma system on whiteleg shrimp (Litopenaeus vannamei), LWT-Food Sci. Technol. 154 (2022) 112547. https://doi.org/10.1016/j.lwt.2021.112547.

[13]

M. Tan, P. Li, W. Yu, et al., Effects of glazing with preservatives on the quality changes of squid during frozen storage, App. Sci. 9(18) (2019) 3847. https://doi.org/10.3390/app9183847.

[14]
Y. Wu, Y. Wu, Advances and trends in food polysaccharide research, Bioact. Carbohydr. Diet. Fibre 28 (2022) 100332. https://doi.org/10.1016/J.BCDF.2022.100332.
DOI
[15]
M. Trigo, A. Rodríguez, G. Dovale, et al., The effect of glazing based on saponin-free quinoa (Chenopodium quinoa) extract on the lipid quality of frozen fatty fish, LWT-Food Sci. Technol. 98 (2018) 231–236. https://doi.org/10.1016/j.lwt.2018.08.031.
DOI
[16]
K. M. Solval, L. A. E. Rodezno, M. Moncada, et al., Evaluation of chitosan nanoparticles as a glazing material for cryogenically frozen shrimp, LWT-Food Sci. Technol. 57(1) (2014) 172–180. https://doi.org/10.1016/j.lwt.2013.12.033.
DOI
[17]

M. Flórez, E. Guerra-Rodríguez, P. Cazón, et al., Chitosan for food packaging: recent advances in active and intelligent films, Food Hydrocoll. 124 (2022) 107328. https://doi.org/10.1016/j.foodhyd.2021.107328.

[18]

H. Wang, S. Pan, S. Wu, Chitooligosaccharides suppress the freeze-denaturation of actomyosin in Aristichthys nobilis surimi protein, Int. J. Biol. Macromol. 63 (2014) 104–106. https://doi.org/10.1016/j.ijbiomac.2013.10.035.

[19]

S. Zhu, J. Yu, X. Chen, et al., Dual cryoprotective strategies for ice-binding and stabilizing of frozen seafood: a review, Trends Food Sci. Tech. 111 (2021) 223–232. https://doi.org/10.1016/j.jpgs.2021.02.069.

[20]
X. F. Xia, B. H. Kong, Q. Liu, et al., Physicochemical change and protein oxidation in porcine Longissimus dorsi as influenced by different freeze-thaw cycles, Meat Sci. 83(2) (2009) 239–245. https://doi.org/10.1016/j.meatsci.2009.05.003.
DOI
[21]

Q. X. Sun, F. D. Sun, X. F. Xia, et al., The comparison of ultrasound-assisted immersion freezing, air freezing and immersion freezing on the muscle quality and physicochemical properties of common carp (Cyprinus carpio) during freezing storage, Ultrason. Sonochem. 51 (2019) 281–291. https://doi.org/10.1016/j.ultsonch.2018.10.006.

[22]

Y. Y. Guo, B. H. Kong, X. F. Xia, et al., Changes in physicochemical and protein structural properties of common carp (Cyprinus carpio) muscle subjected to different freeze-thaw cycles, J. Aquat. Food Prod. T. 23(6) (2014) 579–590. https://doi.org/10.1080/10498850.2012.741663.

[23]

X. Du, M. N. Zhao, N. Pan, et al., Tracking aggregation behaviour and gel properties induced by structural alterations in myofibrillar protein in mirror carp (Cyprinus carpio) under the synergistic effects of pH and heating, Food Chem. 362 (2021) 130222. https://doi.org/10.1016/j.foodchem.2021.130222.

[24]

Y. Cao, Y. Xiong, Chlorogenic acid-mediated gel formation of oxidatively stressed myofibrillar protein, Food Chem. 180 (2015) 235–243. https://doi.org/10.1016/j.foodchem.2015.02.036.

[25]
M. Tan, Z. Liu, Y. Zu, et al., Effect of multiple freeze-thaw cycles on the quality of instant sea cucumber: emphatically on water status of by LF-NMR and MRI, Food Res. Int. 109 (2018) 65–71. https://doi.org/10.1016/j.foodres.2018.04.029.
DOI
[26]
F. F. Li, Q. Zhong, B. H. Kong, et al., Deterioration in quality of quick-frozen pork patties induced by changes in protein structure and lipid and protein oxidation during frozen storage, Food Res. Int. 133 (2020) 09142. https://doi.org/10.1016/j.foodres.2020.109142.
DOI
[27]
M. Nikoo, S. Benjakul. Potential application of seafood-derived peptides as bifunctional ingredients, antioxidant-cryoprotectant: a review, J. Func. Foods 19 (2015) 753–764. https://doi.org/10.1016/j.jff.2015.10.014.
DOI
[28]

X. Yang, A. Li, X. Li, et al., An overview of classifications, properties of food polysaccharides and their links to applications in improving food textures, Trends Food Sci. Tech. 102 (2020) 1–15. https://doi.org/10.1016/j.jpgs.2020.05.020.

[29]

S. Dey, K. Dora, Suitability of chitosan as cryoprotectant on croaker fish (Johnius gangeticus) surimi during frozen storage, J. Food Sci. Technol. 48 (2011) 699–705. https://doi.org/10.1007/s13197-010-0197-8.

[30]

F. F. Li, X. Du, B. Wang, et al., Inhibiting effect of ice structuring protein on the decreased gelling properties of protein from quick-frozen pork patty subjected to frozen storage, Food Chem. 353(2) (2021) 129104. https://doi.org/10.1016/j.foodchem.2021.129104.

[31]

X. Chen, X. Li, F. Yang, et al., Effects and mechanism of antifreeze peptides from silver carp scales on the freeze-thaw stability of frozen surimi, Food Chem. 396 (2022) 133717. https://doi.org/10.1016/j.foodchem.2022.133717.

[32]

D. Chevalier, A. Sequeira-Munoz, A. Bail, et al., Effect of freezing conditions and storage on ice crystal and drip volume in turbot (Scophthalmus maximus): evaluation of pressure shift freezing vs. air-blast freezing, Innov. Food Sci. Emerg. 1 (2000) 193–201. https://doi.org/10.1016/S1466-8564(00)00024-2.

[33]
J. Y. Jeong, G. D. Kim, H. S. Yang, er al., Effect of freeze-thaw cycles on physicochemical properties and color stability of beef semimembranosus muscle, Food Res. Int. 44(10) (2011) 3222–3228. https://doi.org/10.1016/j.foodres.2011.08.023.
DOI
[34]

N. M. Soares, T. S. Mendes, A. A. Vicente, Effect of chitosan-based solutions applied as edible coatings and water glazing on frozen salmon preservation-A pilot-scale study, J. Food Eng. 119(2) (2013) 316–323. https://doi.org/10.1016/j.jfoodeng.2013.05.018.

[35]

M. Gutierrez, C. Oliveira, F. Melo, et al., Limit growth of ice crystals under different temperature oscillations levels in Nile tilapia, Food Sci. Tech. 37 (2017) 673–680. https://doi.org/10.1590/1678-457X.29416.

[36]
X. Sun, Y. Wu, Z. Song, et al., A review of natural polysaccharides for food cryoprotection: ice crystals inhibition and cryo-stabilization, Bioact. Carbohydr. Diet. Fibre 27 (2022) 100291. https://doi.org/10.1016/j.bcdf.2021.100291.
DOI
[37]

Y. Zhang, Y. Kim, E. Puolanne, et al., Role of freezing-induced myofibrillar protein denaturation in the generation of thaw loss: a review, Meat Sci. 190 (2022) 108841. https://doi.org/10.1016/j.meatsci.2022.108841.

[38]

P. Haris, F. Severcan, FTIR spectroscopic characterization of protein structure in aqueous and non-aqueous media, J. Mol. Catal. B-Enzym. 7 (1999) 207–221. https://doi.org/10.1016/S1381-1177(99)00030-2.

[39]
X. Bai, S. Shi, B. H. Kong, et al., Analysis of the influencing mechanism of the freeze-thawing cycles on in vitro chicken meat digestion based on protein structural changes, Food Chem. 399(1) (2022) 134020. https://doi.org/10.1016/j.foodchem.
DOI
[40]

D. Li, S. Jia, L. Zhang, et al., Effect of using a high voltage electrostatic field on microbial communities, degradation of adenosine triphosphate, and water loss when thawing lightly-salted frozen common carp (Cyprinus carpio), J. Food Eng. 212 (2017) 226–233. https://doi.org/10.1016/j.jfoodeng.2017.06.003.

[41]

J. Zhao, F. Dong, Y. Li, et al., Effect of freeze-thaw cycles on the emulsion activity and structural characteristics of soy protein isolate, Process Biochem. 50(10) (2015) 1607–1613. https://doi.org/10.1016/j.procbio.2015.06.021.

[42]

Y. Zhang, L. Chen, S. Lv, et al., Inhibition of interaction between epigallocatechin-3-gallate and myofibrillar protein by cyclodextrin derivatives improves gel quality under oxidative stress, Food Res. Int. 108 (2018) 8–17. https://doi.org/10.1016/j.foodres.2018.03.00.

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Publication history

Received: 27 April 2023
Revised: 22 May 2023
Accepted: 14 June 2023
Published: 17 August 2023
Issue date: June 2023

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© Beijing Academy of Food Sciences 2023.

Acknowledgements

Acknowledgements

This study was supported by the National Natural Science Foundation of China (grant No. 32202104), Northeast Forestry University’s research funding for talent introduced (grant No. 60201520109) and Special Funds for the Basic Scientific Research Expenses of Central Government Universities (grant No. 2572021BA09).

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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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