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dc.contributor.authorHuang, Z.
dc.contributor.authorWang, Yaling
dc.contributor.authorSun, Lijun
dc.contributor.authorWang, X.
dc.contributor.authorLu, P.
dc.contributor.authorLiang, G.
dc.contributor.authorPang, H.
dc.contributor.authorWu, Q.
dc.contributor.authorGooneratne, Sarojith R.
dc.contributor.authorZhao, Jian
dc.date.accessioned2020-01-16T21:06:20Z
dc.date.available2019-08-22en
dc.date.issued2019-08-23
dc.identifier.issn0022-5142en
dc.identifier.urihttps://hdl.handle.net/10182/11306
dc.description.abstractBACKGROUND: T-2 toxin (T-2) is a potent mycotoxin and a common contaminant of aquatic animal feed, posing a serious risk to health and aquatic animals. We investigated the effect of T-2 on shrimp muscle proteins using proteomics and conventional biochemical methods. Shrimp were fed a diet containing T-2 at 0–12.2 mg kg⁻¹ for 20 days, and changes to the muscle protein composition, ATPase activities, and the sulfhydryl (SH) content and hydrophobicity of actomyosin (AM) were determined. A proteomics study of the proteins was conducted with sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), two-dimensional (2D) electrophoresis, and matrix-assisted laser desorption/ionization – time of flight mass spectrometry (MALDI-TOF/TOF MS). RESULTS: Exposure to T-2 markedly affected the muscle protein composition of shrimp in a concentration-responsive manner that displayed a diphasic effect. At a low T-2 concentration (1.2 mg kg⁻¹), the levels of three major muscle proteins (myofibrillar, sarcoplasmic, and stroma) increased but at higher concentrations they declined progressively. T-2 exposure also led to a breakdown of muscle proteins as evidenced by increases in alkali-soluble protein and the surface hydrophobicity (SoANS) of AM. Thirty differentially expressed proteins were detected, 12 of which showed a concentration response relationship with T-2 exposure. Among them, 11 homologous proteins were identified by mass spectrometry (MS), with several being key enzymes in energy metabolism. CONCLUSION: This study demonstrated that T-2 exposure at medium to high concentrations could significantly affect the protein composition and quality of shrimp muscle, and potentially some of its key metabolisms. One of the arginine kinases (spot 27) was particularly responsive to T-2 and could potentially be used as a biomarker protein for T-2 intoxication by shrimp.en
dc.format.extent10en
dc.languageenen
dc.language.isoen
dc.publisherSociety of Chemical Industry
dc.relationThe original publication is available from - Society of Chemical Industry - https://doi.org/10.1002/jsfa.10001en
dc.relation.urihttps://doi.org/10.1002/jsfa.10001en
dc.rights© 2019 Society of Chemical Industry
dc.subjectLitopenaeus vannameien
dc.subjectT-2 toxinen
dc.subjectshrimpen
dc.subjectprotein qualityen
dc.subjectproteomicsen
dc.subjectFood Scienceen
dc.subject.meshMusclesen
dc.subject.meshAnimalsen
dc.subject.meshPenaeidaeen
dc.subject.meshMuscle Proteinsen
dc.subject.meshElectrophoresis, Polyacrylamide Gelen
dc.subject.meshSpectrometry, Mass, Matrix-Assisted Laser Desorption-Ionizationen
dc.subject.meshAnimal Feeden
dc.subject.meshShellfishen
dc.titleEffects of T‐2 toxin on the muscle proteins of shrimp (Litopenaeus vannamei) – a proteomics studyen
dc.typeJournal Article
lu.contributor.unitLincoln University
lu.contributor.unitFaculty of Agriculture and Life Sciences
lu.contributor.unitDepartment of Wine, Food and Molecular Biosciences
dc.identifier.doi10.1002/jsfa.10001en
dc.relation.isPartOfJournal of the Science of Food and Agricultureen
pubs.organisational-group/LU
pubs.organisational-group/LU/Agriculture and Life Sciences
pubs.organisational-group/LU/Agriculture and Life Sciences/WFMB
pubs.organisational-group/LU/Research Management Office
pubs.organisational-group/LU/Research Management Office/QE18
pubs.publication-statusPublished onlineen
dc.identifier.eissn1097-0010en
lu.identifier.orcid0000-0002-5406-2894


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