Proteomics analysis as an approach to understand the formation of pale, soft, and exudative (PSE) pork

Zequan, Xu; Shao, Yi; Guangjuan, Liu; Xing, Shijun; Li, Zhang; Zhu, Mingrui; Xü, Yanli; Wang, Zirong

doi:10.1016/j.meatsci.2020.108353

Cited by 32 publications

(29 citation statements)

References 71 publications

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“…Malate dehydrogenase is an oxidoreductase with NAD or NADP as the receptor, which can catalyze the conversion of L-malic acid to oxaloacetic acid in the TCA cycle. 27 It can be inferred from the above results that the TCA process and malate dehydrogenase expression can be affected by the assistance of AEF during aging.…”

Section: ■ Results and Discussionmentioning

confidence: 99%

“…The main route of oxidation of the carbon skeleton of amino acids is the TCA cycle in which pyruvate is metabolized. 27 In addition, in the process of frozen storage metabolism, energy is generated mainly through glycolytic metabolism, thus participating in thermogenesis. 27 The DAPs of the EA versus FA comparison were mainly enriched in the metabolic pathways and ribosome.…”

Section: ■ Results and Discussionmentioning

confidence: 99%

“…27 In addition, in the process of frozen storage metabolism, energy is generated mainly through glycolytic metabolism, thus participating in thermogenesis. 27 The DAPs of the EA versus FA comparison were mainly enriched in the metabolic pathways and ribosome. This may be because the vibration and collision caused by AEF interfere with the formation and damage of ribosomes.…”

Section: ■ Results and Discussionmentioning

confidence: 99%

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Effects of Alternating Electric Field Assisted Freezing–Thawing–Aging Sequence on Data-Independent Acquisition Quantitative Proteomics of Longissimus dorsi Muscle

Yang

Bruce

et al. 2022

J. Agric. Food Chem.

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This study was designed to investigate the differences in the proteomes of bovine Longissimus dorsi (LD) muscle during an alternating electric field (AEF)-assisted freezing−thawing−aging sequence based on a data-independent acquisition strategy. When compared to that of the only postmortem aging (OA) group, the meat quality of the freezing−thawing−aging sequence (FA) and AEF-assisted freezing−thawing−aging sequence (EA) groups showed a declining trend. However, the group assisted by AEF was significantly enhanced in color, water-holding capacity, and tenderness. Three hundred fifty-two proteins in LD muscle were differentially abundant proteins (DAPs) among FA, EA, and OA treatments. Furthermore, among the 40 DAPs in the FA versus EA comparison, 5 DAPs with variable importance in projection scores higher than 1 were identified as biochemical markers of beef quality. Bioinformatic analysis revealed that most of these proteins were involved in structural constituents of ribosome and catalytic activity. These results provide a basis for further understanding the quality of beef following a freezing− thawing−aging sequence assisted by AEF.

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Section: ■ Results and Discussionmentioning

confidence: 99%

Section: ■ Results and Discussionmentioning

confidence: 99%

Section: ■ Results and Discussionmentioning

confidence: 99%

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Effects of Alternating Electric Field Assisted Freezing–Thawing–Aging Sequence on Data-Independent Acquisition Quantitative Proteomics of Longissimus dorsi Muscle

Yang

Bruce

et al. 2022

J. Agric. Food Chem.

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“…Breast muscle samples from the RFN group showed lower drip loss (2.19 vs. 2.66%, P < 0.05) compared to breast samples from the PSE group. Nam et al (2009) reported that consumers are generally able to distinguish meat in unacceptable condition, especially PSE meat, due to its paler color and large amount of exudated water on the meat surface compared to meat in normal conditions ( Livisay et al, 1996 ; Zequan et al, 2021 ). The occurrence of PSE meat is accompanied by economic losses for the meat industry as a result of its higher moisture loss and decreased purchases due to it's lower appearance acceptability ( Kuttappan et al, 2012 ).…”

Section: Resultsmentioning

confidence: 99%

Research Note: PSE condition is associated with increased apoptotic potential in broiler pectoralis major muscle

Lee

Choi²

2022

Poultry Science

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“…As the water loss of the myocytes reaches a certain extent, the filaments become thinner, and the reflectance of incident light declines, resulting in paleness [ 1 ]. If exposed to high temperatures, the muscle protein denaturation would accelerate [ 6 ], leading to further paleness and lower water holding capacity (WHC) [ 7 ].…”

Section: Introductionmentioning

confidence: 99%

Comparative Study on Pale, Soft and Exudative (PSE) and Red, Firm and Non-Exudative (RFN) Pork: Protein Changes during Aging and the Differential Protein Expression of the Myofibrillar Fraction at 1 h Postmortem

et al. 2021

Foods

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In this paper, the protein changes during aging and the differences in the myofibrillar protein fraction at 1 d postmortem of pale, soft and exudative (PSE), and red, firm and non-exudative (RFN) pork longissimus thoracis (LT) were comparatively studied. The PSE and RFN groups were screened out based on the differences in their pH and lightness (L*) at 1 h, and their purge loss at 24 h postmortem. Based on the measured MFI, desmin degradation, and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) analysis, PSE meat presented more significant changes in the myofibrillar protein fraction compared to RFN meat during postmortem aging. Through liquid chromatograph-mass spectrometer/mass spectrometer (LC-MS/MS) analysis, a total of 172 differential proteins were identified, among which 151 were up-regulated and 21 were down-regulated in the PSE group. The differential proteins were muscle contraction, motor proteins, microfilaments, microtubules, glycolysis, glycogen metabolism, energy metabolism, molecular chaperones, transport, and enzyme proteins. The AMP activated protein kinase (AMPK) signaling pathway, HIF-1 signaling pathway, calcium signaling pathway, and PI3K-Akt signaling pathway were identified as the significant pathways related to meat quality. This study suggested that the different changes of the myofibrillar protein fraction were involved in the biochemical metabolism in postmortem muscle, which may contribute to the molecular understanding of PSE meat formation.

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Proteomics analysis as an approach to understand the formation of pale, soft, and exudative (PSE) pork

Cited by 32 publications

References 71 publications

Effects of Alternating Electric Field Assisted Freezing–Thawing–Aging Sequence on Data-Independent Acquisition Quantitative Proteomics of Longissimus dorsi Muscle

Effects of Alternating Electric Field Assisted Freezing–Thawing–Aging Sequence on Data-Independent Acquisition Quantitative Proteomics of Longissimus dorsi Muscle

Research Note: PSE condition is associated with increased apoptotic potential in broiler pectoralis major muscle

Comparative Study on Pale, Soft and Exudative (PSE) and Red, Firm and Non-Exudative (RFN) Pork: Protein Changes during Aging and the Differential Protein Expression of the Myofibrillar Fraction at 1 h Postmortem

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