Molecular Understanding of Meat Quality Through Application of Proteomics

Wu, Wei; Fu, Yu; Therkildsen, Margrethe; Li, Xingmin; Dai, Ruitong

doi:10.1080/87559129.2014.961073

Cited by 49 publications

(19 citation statements)

References 70 publications

(64 reference statements)

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“…Rapid development of proteomics involves the application of various electrophoretic techniques [12,14,52,55], which allow the identification of many proteins with respect to their properties. It leads to better understanding of the causes and consequences of the phenomena influencing the quality of meat, especially its tenderness [15,20,22,31,32,35,40,47,51].…”

Section: Introductionmentioning

confidence: 99%

The relationship between protein changes in porcine longissimus muscle at different courses of meat tenderisation

Grześ

Pośpiech

Iwańska

et al. 2017

Eur Food Res Technol

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Section: Introductionmentioning

confidence: 99%

The relationship between protein changes in porcine longissimus muscle at different courses of meat tenderisation

Grześ

Pośpiech

Iwańska

et al. 2017

Eur Food Res Technol

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“…The phosphorylation levels of bands 5 and 12 were reduced postmortem in four groups. Heat shock protein 90 beta family member 1 (band 5) is a molecular chaperone closely associated with tenderness . The phosphorylation level of band 5 was positively correlated ( P < 0.05) with ATP content, indicating that heat shock protein is an ATP‐dependent chaperone.…”

Section: Resultsmentioning

confidence: 99%

“…Heat shock protein 90 beta family member 1 (band 5) is a molecular chaperone closely associated with tenderness. 30 The phosphorylation level of band 5 was positively correlated (P < 0.05) with ATP content, indicating that heat shock protein is an ATP-dependent chaperone. Myosin light chain 1, myosin light chain 3 and myosin light chain 6 were identified in band 15.…”

Section: Analysis Of the Phosphorylation Levels Of Individual Bands Amentioning

confidence: 92%

Effects of temperature on protein phosphorylation in postmortem muscle

Ren

Hou

et al. 2019

J Sci Food Agric

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BACKGROUND Phosphorylation is one of the most important post‐translational modifications. Currently, many postmortem protein phosphorylation studies in muscle have been related to meat quality such as tenderness and color stability. However, the effects of various storage temperatures (25, 15, 4 and −1.5 °C) on the phosphorylation level of protein are poorly understood. Changes in the protein phosphorylation levels in postmortem ovine muscle at various storage temperatures were determined in this study. RESULTS The obtained data showed that pH decline rate was significantly inhibited at −1.5 °C from 12 h to 7 days postmortem (P < 0.05). The ATP consumption rate was higher at 25 °C than that at other three temperatures (P < 0.05). Analysis of the temperature, pH and ATP content revealed that the ATP content was related to the phosphorylation levels of individual protein bands. Phosphorylated myofibrillar and sarcoplasmic proteins, such as myosin binding protein C, troponin T3, myosin light chain 1, glucose‐6‐phosphate isomerase and pyruvate kinase, were mainly involved in glycolysis and muscle contraction. CONCLUSION The global and specific protein phosphorylation levels can be influenced by the postmortem storage temperature of muscle. Phosphorylation of proteins was correlated with glycolysis and muscle contraction. Certain phosphorylated proteins, such as heat shock proteins, require further study to clarify their effects on meat traits. © 2019 Society of Chemical Industry

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“…Proteome is exceedingly dynamic and continuously variable field in response to cellular or environmental factors, influencing either synthesis or degradation of protein compared to the static genome. 18 Studies on genes alone do not provide much information. Reflection on phenotypes of cells is monitored with focusing on proteins, not genes.…”

Section: Applications Of Proteomicsmentioning

confidence: 99%

A Smart Way for Talking With Proteins; Proteomics

Zengin

Kiliç

Yenigün

et al. 2017

MOJPB

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Proteomics is the large-scale analysis of proteins, contributing for understanding of gene function. Functional genomics, proteomics, and even metabolomics are the footsteps of genomics that are useful tool to expand of our knowledge on the biological hierarchy of the transcription, translation, and production of small molecules. However, proteomics is a method for assessing the wide range of information such as the structure, expression, localization, biochemical activity, interactions, posttranslational modifications and cellular roles of proteins following protein isolation, digestion and mass spectrometry. Proteomics, as a significant post-genomic tool in the field of science, allows researchers to decipher underlying molecular mechanisms behind different metabolic pathways. Proteomics studies are mostly based on protein identification as using mainly bottom-up approaches such as DDA or MudPIT methods as examples of shotgun proteomics techniques. By using the high throughput mass spectrometer technology, huge output data of peptide spectra has been generated.

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Molecular Understanding of Meat Quality Through Application of Proteomics

Cited by 49 publications

References 70 publications

The relationship between protein changes in porcine longissimus muscle at different courses of meat tenderisation

The relationship between protein changes in porcine longissimus muscle at different courses of meat tenderisation

Effects of temperature on protein phosphorylation in postmortem muscle

A Smart Way for Talking With Proteins; Proteomics

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