Cold-induced denaturation of muscle proteins in hairtail (Trichiurus lepturus) during storage: Physicochemical and label-free based proteomics analyses

9 pages, 4 figures.-- Under a Creative Commons license

Bibliographic Details
Authors: Shui, Shan-Shan, Yan, Hongbo, Tu, Chuanhai, Benjakul, Soottawat, Aubourg, Santiago P., Zhang, Bin
Format: article
Status:Published version
Publication Date:2022
Country:España
Institution:Consejo Superior de Investigaciones Científicas (CSIC)
Repository:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/282247
Online Access:http://hdl.handle.net/10261/282247
Access Level:Open access
Keyword:Hairtail
Protein denaturation
Proteomics
Cold stress
Cytoskeletal proteins
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spelling Cold-induced denaturation of muscle proteins in hairtail (Trichiurus lepturus) during storage: Physicochemical and label-free based proteomics analysesShui, Shan-ShanYan, HongboTu, ChuanhaiBenjakul, SoottawatAubourg, Santiago P.Zhang, BinHairtailProtein denaturationProteomicsCold stressCytoskeletal proteins9 pages, 4 figures.-- Under a Creative Commons licensePhysicochemical, proteomics, and bioinformatics analyses were conducted to investigate protein profiles in Trichiurus haumela under frozen (120 d) and chilled (6 d) storage. Springiness, chewiness, myofibrillar active sulfhydryl content, and Ca2+-ATPase activity significantly decreased, suggesting that cold stress altered muscle proteins. Compared with fresh hairtail (FH), 66 common differentially abundant proteins (DAPs) had lower abundances in chilled (3 d; CSH) and frozen (120 d; FSH) hairtail, including myosin binding proteins, filamins, actinin, troponin, and muscle-restricted coiled-coil protein. Gene Ontology (GO) annotation showed DAPs were mainly involved in cellular process, cellular anatomical entity, intracellular, and binding items. Eukaryotic orthologous group (KOG) analysis revealed that changes in cytoskeleton and energy production and conversion functions dominated during cold storage, degrading the myofibril and connective tissue structures and the physicochemical performance of muscle tissues. This study presents deep insights into the protein alternation mechanisms in hairtail muscle under cold stressThis study was funded by the National Natural Science Foundation of China (No. 32072146), the Zhejiang Natural Science Foundation of China (No. LR21C200001), the Zhejiang Leading Training Program (2020R52027), and the Fundamental Research Funds of Zhejiang Province (2021JD005)Peer reviewedElsevierNational Natural Science Foundation of ChinaZhejiang Provincial Natural Science FoundationScience and Technology Department of Zhejiang ProvinceConsejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]202220222022info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Publisher's versioninfo:eu-repo/semantics/publishedVersionhttp://hdl.handle.net/10261/282247reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)InglésData will be made available on requesthttps://doi.org/10.1016/j.fochx.2022.100479Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/2822472026-05-22T06:33:51Z
dc.title.none.fl_str_mv Cold-induced denaturation of muscle proteins in hairtail (Trichiurus lepturus) during storage: Physicochemical and label-free based proteomics analyses
title Cold-induced denaturation of muscle proteins in hairtail (Trichiurus lepturus) during storage: Physicochemical and label-free based proteomics analyses
spellingShingle Cold-induced denaturation of muscle proteins in hairtail (Trichiurus lepturus) during storage: Physicochemical and label-free based proteomics analyses
Shui, Shan-Shan
Hairtail
Protein denaturation
Proteomics
Cold stress
Cytoskeletal proteins
title_short Cold-induced denaturation of muscle proteins in hairtail (Trichiurus lepturus) during storage: Physicochemical and label-free based proteomics analyses
title_full Cold-induced denaturation of muscle proteins in hairtail (Trichiurus lepturus) during storage: Physicochemical and label-free based proteomics analyses
title_fullStr Cold-induced denaturation of muscle proteins in hairtail (Trichiurus lepturus) during storage: Physicochemical and label-free based proteomics analyses
title_full_unstemmed Cold-induced denaturation of muscle proteins in hairtail (Trichiurus lepturus) during storage: Physicochemical and label-free based proteomics analyses
title_sort Cold-induced denaturation of muscle proteins in hairtail (Trichiurus lepturus) during storage: Physicochemical and label-free based proteomics analyses
dc.creator.none.fl_str_mv Shui, Shan-Shan
Yan, Hongbo
Tu, Chuanhai
Benjakul, Soottawat
Aubourg, Santiago P.
Zhang, Bin
author Shui, Shan-Shan
author_facet Shui, Shan-Shan
Yan, Hongbo
Tu, Chuanhai
Benjakul, Soottawat
Aubourg, Santiago P.
Zhang, Bin
author_role author
author2 Yan, Hongbo
Tu, Chuanhai
Benjakul, Soottawat
Aubourg, Santiago P.
Zhang, Bin
author2_role author
author
author
author
author
dc.contributor.none.fl_str_mv National Natural Science Foundation of China
Zhejiang Provincial Natural Science Foundation
Science and Technology Department of Zhejiang Province
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv Hairtail
Protein denaturation
Proteomics
Cold stress
Cytoskeletal proteins
topic Hairtail
Protein denaturation
Proteomics
Cold stress
Cytoskeletal proteins
description 9 pages, 4 figures.-- Under a Creative Commons license
publishDate 2022
dc.date.none.fl_str_mv 2022
2022
2022
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
Publisher's version
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/282247
url http://hdl.handle.net/10261/282247
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Data will be made available on request
https://doi.org/10.1016/j.fochx.2022.100479
Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
repository.name.fl_str_mv
repository.mail.fl_str_mv
_version_ 1869415808296288256
score 15.812455

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