Investigation of the Sarcoplasmic Proteome Contribution to the Development of Pork Loin Tenderness
dc.contributor.author | Schulte, Matthew D. | |
dc.contributor.author | Johnson, Logan G. | |
dc.contributor.author | Zuber, Elizabeth A. | |
dc.contributor.author | Steadham, Edward M. | |
dc.contributor.author | King, D. Andy | |
dc.contributor.author | Huff-Lonergan, Elisabeth | |
dc.contributor.author | Lonergan, Steven | |
dc.contributor.department | Animal Science | |
dc.date.accessioned | 2022-03-24T16:52:30Z | |
dc.date.available | 2022-03-24T16:52:30Z | |
dc.date.issued | 2020 | |
dc.description.abstract | The study objectives were to determine the extent to which the sarcoplasmic proteome explains variations in aged pork loin star probe value. Pork loins (n=12) were categorized by differences in star probe at 21 d post mortem from a larger set of loins. Loins were categorized into low star probe (LSP) group (n=6; star probe<5.80 kg) and high star probe (HSP) group (n=6; star probe>7.00 kg) based on 21-d star probe value with inclusion criteria of marbling score (1.0–3.0) and 24-h pH (5.69–5.98). Quality traits were measured at 1-, 8-, 14-, and 21-d aging. Desmin and troponin-T degradation, peroxiredoxin-2 abundance, calpain-1 autolysis, and sarcomere length were determined. Two-dimensional difference gel electrophoresis and mass spectrometry were used to identify proteins that differed in abundance due to category. Star probe values were lower (P<0.01) in LSP at each day of aging compared with HSP. Greater pH values were observed (P<0.05)in LSP compared with HSP at each day of aging. Marbling score was greater (P<0.05) in LSP compared with HSP at each day of aging. Greater (P<0.05) desmin and troponin-T degradation was detected in LSP chops at 14- and 21-d aging and 8-, 14-, and 21-d aging, respectively. Greater (P<0.05) sarcomere length was determined in LSP compared with HSP at 1-,8-, and 21-d aging. Sarcoplasmic proteins from HSP chops had greater abundance (P<0.10) of metabolic and regulatory proteins, whereas the LSP chops had greater abundance (P<0.10) of stress response proteins. Star probe values were affected by pH, marbling score, protein degradation, sarcomere length, and sarcoplasmic proteome. | |
dc.description.comments | This article is published as Schulte, M. D. & Johnson, L. G. & Zuber, E. A. & Steadham, E. M. & King, D. A. & Huff-Lonergan, E. J. & Lonergan, S. M., (2020) “Investigation of the Sarcoplasmic Proteome Contribution to the Development of Pork Loin Tenderness”, Meat and Muscle Biology 4(1). doi: https://doi.org/10.22175/mmb.9566. Works produced by employees of the U.S. Government as part of their official duties are not copyrighted within the U.S. The content of this document is not copyrighted. | |
dc.identifier.uri | https://dr.lib.iastate.edu/handle/20.500.12876/KrZJblqr | |
dc.language.iso | en | |
dc.source.uri | https://doi.org/10.22175/mmb.9566 | * |
dc.subject.keywords | stress response proteins | |
dc.subject.keywords | proteolysis | |
dc.subject.keywords | pork quality | |
dc.subject.keywords | glycolytic proteins | |
dc.title | Investigation of the Sarcoplasmic Proteome Contribution to the Development of Pork Loin Tenderness | |
dc.type | Article | |
dspace.entity.type | Publication | |
relation.isAuthorOfPublication | 6a8e1178-0f76-46eb-bf7a-9f871232456b | |
relation.isAuthorOfPublication | 8e04bc80-6e32-476c-a184-b0311cebe213 | |
relation.isOrgUnitOfPublication | 85ecce08-311a-441b-9c4d-ee2a3569506f |
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