Label-free based proteomics revealed the specific changes of muscle proteins in pike eel (Muraenesox cinereus) under cold stress
Chemical- and liquid chromatography coupled with mass spectrometry (LC–MS) based proteomics strategies were executed to investigate the alterations of protein profiles in pike eel (Muraenesox cinereus) muscle during chilling (CPE) and frozen (FPE) storage. Chemical results indicated that springiness...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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Elsevier
2022-06-01
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| Series: | Food Chemistry: X |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2590157522000736 |
| _version_ | 1811242664264204288 |
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| author | Pengxiang Yuan Xiaonan Chen Soottawat Benjakul Jipeng Sun Bin Zhang |
| author_facet | Pengxiang Yuan Xiaonan Chen Soottawat Benjakul Jipeng Sun Bin Zhang |
| author_sort | Pengxiang Yuan |
| collection | DOAJ |
| description | Chemical- and liquid chromatography coupled with mass spectrometry (LC–MS) based proteomics strategies were executed to investigate the alterations of protein profiles in pike eel (Muraenesox cinereus) muscle during chilling (CPE) and frozen (FPE) storage. Chemical results indicated that springiness and myofibrillar protein (MP) content of muscle tissues decreased significantly during 6 days of chilled and 120 days of frozen storage. LC–MS-based proteomics analysis suggested that great alterations occurred in muscle proteins mainly induced by cold stress. The differentially abundant proteins (DAPs) with low abundances in CPE and FPE samples included the annexins, fibronectin, ribosomal proteins, T-complex proteins, tubulin beta chain, and histones, which were mostly associated with the membrane structural constituents, cytoskeleton, and binding functional proteins. Results of eukaryotic cluster of orthologous group (KOG) verified that these identified DAPs were mainly converged in the cytoskeleton function resulting from cold conditions, which in turn affected the physical structure and chemical performances of muscle tissues. |
| first_indexed | 2024-04-12T13:55:19Z |
| format | Article |
| id | doaj.art-ed278fc632c74f67938fba339d8ed1d3 |
| institution | Directory Open Access Journal |
| issn | 2590-1575 |
| language | English |
| last_indexed | 2024-04-12T13:55:19Z |
| publishDate | 2022-06-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Food Chemistry: X |
| spelling | doaj.art-ed278fc632c74f67938fba339d8ed1d32022-12-22T03:30:24ZengElsevierFood Chemistry: X2590-15752022-06-0114100275Label-free based proteomics revealed the specific changes of muscle proteins in pike eel (Muraenesox cinereus) under cold stressPengxiang Yuan0Xiaonan Chen1Soottawat Benjakul2Jipeng Sun3Bin Zhang4Key Laboratory of Health Risk Factors for Seafood of Zhejiang Province, College of Food Science and Pharmacy, Zhejiang Ocean University, ChinaKey Laboratory of Health Risk Factors for Seafood of Zhejiang Province, College of Food Science and Pharmacy, Zhejiang Ocean University, ChinaInternational Center of Excellence in Seafood Science and Innovation, Faculty of Agro-Industry, Prince of Songkla University, ThailandZhejiang Marine Development Research Institute, China; Corresponding authors at: No.1, Haida South Road, Lincheng Changzhi Island, Zhoushan, Zhejiang Province 316022, China.Key Laboratory of Health Risk Factors for Seafood of Zhejiang Province, College of Food Science and Pharmacy, Zhejiang Ocean University, China; Pisa Marine Graduate School, Zhejiang Ocean University, China; Corresponding authors at: No.1, Haida South Road, Lincheng Changzhi Island, Zhoushan, Zhejiang Province 316022, China.Chemical- and liquid chromatography coupled with mass spectrometry (LC–MS) based proteomics strategies were executed to investigate the alterations of protein profiles in pike eel (Muraenesox cinereus) muscle during chilling (CPE) and frozen (FPE) storage. Chemical results indicated that springiness and myofibrillar protein (MP) content of muscle tissues decreased significantly during 6 days of chilled and 120 days of frozen storage. LC–MS-based proteomics analysis suggested that great alterations occurred in muscle proteins mainly induced by cold stress. The differentially abundant proteins (DAPs) with low abundances in CPE and FPE samples included the annexins, fibronectin, ribosomal proteins, T-complex proteins, tubulin beta chain, and histones, which were mostly associated with the membrane structural constituents, cytoskeleton, and binding functional proteins. Results of eukaryotic cluster of orthologous group (KOG) verified that these identified DAPs were mainly converged in the cytoskeleton function resulting from cold conditions, which in turn affected the physical structure and chemical performances of muscle tissues.http://www.sciencedirect.com/science/article/pii/S2590157522000736Pike eelProtein stabilityAlterationLabel-free proteomicsCold storage |
| spellingShingle | Pengxiang Yuan Xiaonan Chen Soottawat Benjakul Jipeng Sun Bin Zhang Label-free based proteomics revealed the specific changes of muscle proteins in pike eel (Muraenesox cinereus) under cold stress Food Chemistry: X Pike eel Protein stability Alteration Label-free proteomics Cold storage |
| title | Label-free based proteomics revealed the specific changes of muscle proteins in pike eel (Muraenesox cinereus) under cold stress |
| title_full | Label-free based proteomics revealed the specific changes of muscle proteins in pike eel (Muraenesox cinereus) under cold stress |
| title_fullStr | Label-free based proteomics revealed the specific changes of muscle proteins in pike eel (Muraenesox cinereus) under cold stress |
| title_full_unstemmed | Label-free based proteomics revealed the specific changes of muscle proteins in pike eel (Muraenesox cinereus) under cold stress |
| title_short | Label-free based proteomics revealed the specific changes of muscle proteins in pike eel (Muraenesox cinereus) under cold stress |
| title_sort | label free based proteomics revealed the specific changes of muscle proteins in pike eel muraenesox cinereus under cold stress |
| topic | Pike eel Protein stability Alteration Label-free proteomics Cold storage |
| url | http://www.sciencedirect.com/science/article/pii/S2590157522000736 |
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