Application of 2-D DIGE to study the effect of ageing on horse meat myofibrillar sub-proteome.

Autor: Beldarrain LR; Lactiker Research Group, Department of Pharmacy & Food Sciences, University of the Basque Country (UPV/EHU), 01006 Vitoria-Gasteiz, Spain.; Instituto de Agroquímica y Tecnología de Alimentos (CSIC), 46980 Paterna, Spain., Sentandreu E; Instituto de Agroquímica y Tecnología de Alimentos (CSIC), 46980 Paterna, Spain., Aldai N; Lactiker Research Group, Department of Pharmacy & Food Sciences, University of the Basque Country (UPV/EHU), 01006 Vitoria-Gasteiz, Spain., Sentandreu MÁ; Instituto de Agroquímica y Tecnología de Alimentos (CSIC), 46980 Paterna, Spain. Electronic address: ciesen@iata.csic.es., Miller I; Institute of Medical Biochemistry, University of Veterinary Medicine Vienna, 1210 Wien, Austria. Electronic address: Ingrid.miller@vetmeduni.ac.at.
Jazyk: angličtina
Zdroj: Journal of proteomics [J Proteomics] 2023 Feb 10; Vol. 272, pp. 104770. Date of Electronic Publication: 2022 Nov 29.
DOI: 10.1016/j.jprot.2022.104770
Abstrakt: Considering the high relevance of meat tenderness for consumer acceptability, the aim of this study was to investigate post-mortem changes in myofibrillar sub-proteome in steaks from longissimus thoracis et lumborum muscle of six Hispano-Bretón horses. Indeed, the ageing process that leads to meat tenderization has been scarcely studied in this species. Steaks (n = 24) were aged (4 °C) in the dark under vacuum for 0, 7, 14 and 21 days and the myofibrillar sub-proteome was extracted. Using 2-D DIGE minimal labelling, 35 spots that were differentially abundant between 0 and 21 days aged meat were detected. Of them, 24 were analysed by LC-MS/MS, identifying a total of 29 equine proteins. These were structural and metabolic proteins, and among them, four (Actin, Troponin T and Myosin binding proteins 1 and 2) were selected for Western blot analysis, reporting changes in their abundance after 0, 7, 14 and 21 days of ageing. Results revealed that they should be further studied as potential protein biomarkers of horse meat tenderization. Additionally, several protein fragments increased after ageing, as was the case of glyceraldehyde-3-phosphate dehydrogenase. Fragments of this protein were present in four protein spots, and their study could be useful for monitoring horse meat tenderization. SIGNIFICANCE: Tenderization during ageing has been widely studied in meat from several farm animal species; however, both research and standardized ageing practices are lacking for the particular case of horse meat. In this regard, this study presents novel proteomic findings related to post-mortem evolution of horse muscle proteins. Acquired knowledge would support the development and optimization of efficient ageing practices by horse meat industry.
Competing Interests: Declaration of Competing Interest Authors declare no conflict of interest.
(Copyright © 2022 The Authors. Published by Elsevier B.V. All rights reserved.)
Databáze: MEDLINE
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