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Food Science of Animal Products 2023, 1(1): 9240002 https://doi.org/10.26599/FSAP.2023.9240002
Research Article | Open Access | Issue | Published: 01 March 2023

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

Show Author's Information 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
Keywords:
Litopenaeus vannamei, protein changes, partial freezing, quality deterioration, bioinformatic analysis
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
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Abstract Full text About this article

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.


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About this article

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

Show Author's information 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

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 vannamei, protein changes, partial freezing, quality deterioration, bioinformatic analysis

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Publication history
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Publication history

Received: 04 December 2022
Revised: 27 December 2022
Accepted: 03 January 2023
Published: 01 March 2023
Issue date: March 2023

Copyright

© Beijing Academy of Food Sciences 2023.

Acknowledgements

This work was supported by the Hainan Provincial Joint Project of Sanya Yazhou Bay Science and Technology City (No. 320LH037), Hainan Provincial Natural Science Foundation (No. 322QN434), the National Natural Science Foundation of China (No. 32072147), and the Guangdong Provincial Special Fund For Modern Agriculture Industry Technology Innovation Teams (No. 2022KJ151).

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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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