AI Chat Paper
Note: Please note that the following content is generated by AMiner AI. SciOpen does not take any responsibility related to this content.
{{lang === 'zh_CN' ? '文章概述' : 'Summary'}}
{{lang === 'en_US' ? '中' : 'Eng'}}
Chat more with AI
Powered by AMiner. Clicking this button will take you away from SciOpen.
Home Food Science of Animal Products Article
PDF (1.7 MB)
Cite
EndNote(RIS) BibTeX
Collect
Submit Manuscript AI Chat Paper
Show Outline
Outline
Show full outline
Hide outline
Outline
Show full outline
Hide outline
Research Article | Open Access

Quality deterioration of Litopenaeus vannamei associated with protein changes during partial freezing storage

Kangting Sun1,2, Chuang Pan1,3( ), Shengjun Chen1,2,3( ), Feiyan Tao1, Shucheng Liu2, Yongqiang Zhao1,3, Chunsheng Li1,3, Di Wang1
Key Laboratory of Aquatic Product Processing, Ministry of Agriculture and Rural Affairs, National R&D Center for Aquatic Product Processing, South China Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Guangzhou 510300, China
College of Food Science and Technology, Guangdong Ocean University, Zhanjiang 524088, China
Key Laboratory of Efficient Utilization and Processing of Marine Fishery Resources of Hainan Province, Sanya Tropical Fisheries Research Institute, Sanya 572018, China
Show Author Information

Abstract

Proteins play a substantial role in the deterioration of partial freezing shrimp product quality. In this study, traditional protein indicators were used to determine changes in shrimp muscle quality during storage, and the changed proteins were identified using proteomic analysis. The decrease in total sulfhydryl (SH) content and the increase in carbonyl content indicate protein is denatured. The decrease in Ca2+-ATPase activity and the increase in surface hydrophobicity also indicate protein denatured. The increase of hydrophobic interaction and disulfide bonds suggest a larger and closer network among proteins. A total of eight changed protein bands were detected on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) diagram under partial freezing storage. Three of them were identified as α-actinin (97 kDa), invertebrate connectin (I-connectin (55 kDa)), and troponin I (30 kDa), respectively, which are essential components of myofibrillar protein. The results of the bioinformatic analysis showed that α-actinin and troponin I are unstable proteins with a secondary structure dominated by α-helix, while I-connectin is a stable protein with a secondary structure dominated by random coil. All three proteins are hydrophilic and predicted to be non-toxic on ToxinPreds.

Keywords

Litopenaeus vannameiprotein changespartial freezingquality deteriorationbioinformatic analysis

References

[1]

B. Zhang, C. D. Fang, G. J. 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.
Crossref Google Scholar
[2]

C. Pan, S. J. Chen, S. X. Hao, et al., Effect of low-temperature preservation on quality changes in Pacific white shrimp, Litopenaeus vannamei: a review, J. Sci. Food Agric. 99(14) (2019) 6121–6128. https://doi.org/10.1002/jsfa.9905.
Crossref Google Scholar
[3]

L. K. Ma, B. Zhang, S. G. Deng, et al., Comparison of the cryoprotective effects of trehalose, alginate, and its oligosaccharides on peeled shrimp (Litopenaeus vannamei) during frozen storage, J. Food Sci. 80(3) (2015) C540–C546. https://doi.org/10.1111/1750-3841.12793.
Crossref Google Scholar
[4]

X. Dong, J. Wang, V. Raghavan, Impact of microwave processing on the secondary structure, in-vitro protein digestibility and allergenicity of shrimp (Litopenaeus vannamei) proteins, Food Chem. 337 (2021) 127811. https://doi.org/10.1016/j.foodchem.2020.127811.
Crossref Google Scholar
[5]

A. Nawaz, Z. Xiong, H. Xiong, et al., The impact of hydrophilic emulsifiers on the physico-chemical properties, microstructure, water distribution and in vitro digestibility of proteins in fried snacks based on fish meat, Food Funct. 10(10) (2019) 6927–6935. https://doi.org/10.1039/c9fo01312a.
Crossref Google Scholar
[6]

C. Pan, K. T. Sun, X. Q. 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 Compos. Anal. 112 (2022) 104655. https://doi.org/10.1016/J.JFCA.2022.104655.
Crossref Google Scholar
[7]

W. N. Ji, Y. L. Bao, K. Y. Wang, et al., Protein changes in shrimp (Metapenaeus ensis) frozen stored at different temperatures and the relation to water-holding capacity, Int. J. Food Sci. Technol. 56(8) (2021) 3924–3937. https://doi.org/10.1111/IJFS.15009.
Crossref Google Scholar
[8]

B. Zhang, S. G. Deng, M. Gao, et al., Effect of slurry ice on the functional properties of proteins related to quality loss during skipjack tuna (Katsuwonus pelamis) chilled storage, J. Food Sci. 80(4) (2015) C695–C702. https://doi.org/10.1111/1750-3841.12812.
Crossref Google Scholar
[9]

S. Benjakul, F. Bauer, Physicochemical and enzymatic changes of cod muscle proteins subjected to different freeze-thaw cycles, J. Sci. Food Agri. 80(8) (2000) 1143–1150. https://doi.org/10.1002/1097-0010(200006)80:8<1143::AID-JSFA610>3.0.CO;2-C.
Crossref Google Scholar
[10]

S. Riebroy, S. Benjakul, W. Visessanguan, et al., Effect of iced storage of bigeye snapper (Priacanthus tayenus) on the chemical composition, properties and acceptability of Som-fug, a fermented Thai fish mince, Food Chem. 102(1) (2006) 270–280. https://doi.org/10.1016/j.foodchem.2006.05.017.
Crossref Google Scholar
[11]

S. Benjakul, M. T. Morrissey, Protein hydrolysates from Pacific whiting solid wastes, J. Sci. Food Agri. 45(9) (1997) 3423–3430. https://doi.org/10.1021/jf970294g.
Crossref Google Scholar
[12]

A. Reza, M. J. Breiding, J. Gulaid, et al., Sexual violence and its health consequences for female children in Swaziland: a cluster survey study, The Lancet 373 (2009) 1966–1972. https://doi.org/10.1016/s0140-6736(09)60247-6.
Crossref Google Scholar
[13]

Q. Liu, Q. Chen, B. H. Kong, et al., The influence of superchilling and cryoprotectants on protein oxidation and structural changes in the myofibrillar proteins of common carp (Cyprinus carpio) surimi, LWT-Food Sci. Technol. 57(2) (2014) 603–611. https://doi.org/10.1016/j.lwt.2014.02.023.
Crossref Google Scholar
[14]

F. Badii, N. K. Howell, A comparison of biochemical changes in cod (Gadus morhua) and haddock (Melanogrammus aeglefinus) fillets during frozen storage, J. Sci. Food Agri. 82(1) (2002) 87–97. https://doi.org/10.1002/jsfa.998.
Crossref Google Scholar
[15]

M. Nikoo, S. Benjakul, K. Rahmanifarah, Hydrolysates from marine sources as cryoprotective substances in seafoods and seafood products, Trends Food Sci. Technol. 57 (2016) 40–51. https://doi.org/10.1016/j.jpgs.2016.09.001.
Crossref Google Scholar
[16]

M. V. M. Chamba, Y. Hua, W. Katiyo, Oxidation and structural modification of full-fat and defatted flour based soy protein isolates induced by natural and synthetic extraction chemicals, Food Biophys. 9(3) (2014) 193–202. https://doi.org/10.1007/s11483-014-9333-8.
Crossref Google Scholar
[17]

E. Mario, Protein carbonyls in meat systems: a review, Meat Sci. 89(3) (2011) 259–279. https://doi.org/10.1016/j.meatsci.2011.04.025.
Crossref Google Scholar
[18]

Y. Sun, L. Ma, M. S. Ma, et al., Texture characteristics of chilled prepared Mandarin fish (Siniperca chuatsi) during storage, Int. J. Food Prop. 21(1) (2018) 242–254. https://doi.org/10.1080/10942912.2018.1451343.
Crossref Google Scholar
[19]

K. Subbaiah, R. K. Majumdar, J. Choudhury, et al., Protein degradation and instrumental textural changes in fresh Nile tilapia (Oreochromis niloticus) during frozen storage, J. Food Process. Preserv. 39(6) (2015) 2206–2214. https://doi.org/10.1111/jfpp.12465.
Crossref Google Scholar
[20]

M. Anese, L. Manzocco, A. Panozzo, et al., Effect of radiofrequency assisted freezing on meat microstructure and quality, Food Res. Int. 46(1) (2012) 50–54. https://doi.org/10.1016/j.foodres.2011.11.025.
Crossref Google Scholar
[21]

I. Papa, C. Alvarez, V. Verrez-Bagnis, et al., Post mortem release of fish white muscle α-actinin as a marker of disorganisation, J. Sci. Food Agri. 72(1) (1996) 63–70. https://doi.org/10.1002/(SICI)1097-0010(199609)72:1<63::AID-JSFA623>3.0.CO;2-B.
Crossref Google Scholar
[22]

P. Ertbjerg, E. Puolanne, Muscle structure, sarcomere length and influences on meat quality: a review, Meat Sci. 132 (2017) 139–152. https://doi.org/10.1016/j.meatsci.2017.04.261.
Crossref Google Scholar
[23]

C. Delbarre-Ladrat, R. Chéret, R. Taylor, et al., Trends in postmortem aging in fish: understanding of proteolysis and disorganization of the myofibrillar structure, Crit. Rev. Food Sci. Nutr. 46(5) (2006) 409–421. https://doi.org/10.1080/10408390591000929.
Crossref Google Scholar
[24]

A. D. Malva, M. Albenzio, A. Santillo, et al., Methods for extraction of muscle proteins from meat and fish using denaturing and nondenaturing solutions, J. Food Qual. (2018) 1–9. https://doi.org/10.1155/2018/8478471.
Crossref Google Scholar
[25]

B. Y. Zhu, M. E. Zhou, C. M. Kay, et al., Packing and hydrophobicity effects on protein folding and stability: effects of β-branched amino acids, valine and isoleucine, on the formation and stability of two-stranded α-helical coiled coils/leucine zippers, Protein Sci. 2(3) (1993) 383–394. https://doi.org/10.1002/pro.5560020310.
Crossref Google Scholar
[26]

P. P. Purslow, M. Gagaoua, R. D. Warner, Insights on meat quality from combining traditional studies and proteomics, Meat Sci. 174 (2021) 108423. https://doi.org/10.1016/j.meatsci.2020.108423.
Crossref Google Scholar
[27]

A. Fukuzawa, J. Shimamura, S. Takemori, et al., Invertebrate connectin spans as much as 3.5 μm in the giant sarcomeres of crayfish claw muscle, EMBO J. 20(17) (2001) 4826–4835. https://doi.org/10.1093/emboj/20.17.4826.
Crossref Google Scholar
[28]

C. Chantarasuwan, S. Benjakul, W. Visessanguan, The effects of sodium bicarbonate on conformational changes of natural actomyosin from Pacific white shrimp (Litopenaeus vannamei), Food Chem. 129(4) (2011) 1636–1643. https://doi.org/10.1016/j.foodchem.2011.06.023.
Crossref Google Scholar
[29]

X. Li, Y. Chen, L. Cai, et al., Freshness assessment of turbot (Scophthalmus maximus) by Quality Index Method (QIM), biochemical, and proteomic methods, LWT-Food Sci. Technol. 78 (2017) 172–180. https://doi.org/10.1016/j.lwt.2016.12.037.
Crossref Google Scholar
[30]

Y. Bao, K. Wang, K. H. Yang, et al., Protein degradation of black carp (Mylopharyngodon piceus) muscle during cold storage, Food Chem. 308 (2020) 125576. https://doi.org/10.1016/j.foodchem.2019.125576.
Crossref Google Scholar
Food Science of Animal Products
Volume 1 Issue 1,
March 2023
Article number: 9240002
DOI: 10.26599/FSAP.2023.9240002
Cite this article:
Sun K, Pan C, Chen S, et al. Quality deterioration of Litopenaeus vannamei associated with protein changes during partial freezing storage. Food Science of Animal Products, 2023, 1(1): 9240002. https://doi.org/10.26599/FSAP.2023.9240002

5179

Views

677

Downloads

0

Crossref

Altmetrics
Received: 04 December 2022
Revised: 27 December 2022
Accepted: 03 January 2023
Published: 01 March 2023
© Beijing Academy of Food Sciences 2023.

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/).
Return