Early post-mortem sarcoplasmic proteome of porcine muscle related to lipid oxidation in aged and cooked meat

Sayd, Thierry; Chambon, Christophe; Laville, Élisabeth; Lebret, Bénédicte; Gilbert, Hélène; Gatellier, Philippe

doi:10.1016/j.foodchem.2012.07.079

Cited by 17 publications

(6 citation statements)

References 36 publications

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“…Another previous study of the early sarcoplasmic protein oxidation of pork after slaughter showed that myoglobin was an effective promoter of myofibril protein oxidation (Sayd et al (2012). Sun et al (2012) found that during protein oxidation, MetMb accumulated in muscles and reacted with H 2 O 2 to form hypervalent (Fe 4+ ) myoglobin-promoting protein oxidation, which was consistent with our correlation analysis of MetMb and protein oxidation.…”

Section: Correlation Analysis Of Myoglobin Color Lipid Oxidation and Protein Oxidationsupporting

confidence: 90%

Influence of bleeding on myoglobin and meat quality changes of Channel catfish muscle during freeze‐thaw cycles

Huang

Wang

Xiong

et al. 2021

J. Food Process. Preserv.

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Channel catfish is a large-scale characteristic freshwater fish imported from the United States, which is tender, scaleless, and easy to process (Wei et al., 2007). Since the scale and technology of processing and preservation are far behind those in America, Japan, and other countries, the keys to achieve sustainable development are to exploit freshwater fish processing and cold chain logistics (Yang & Li, 2011). In the long-distance transportation, storage, and consumption of aquatic products, inevitably repeated freezing and thawing due to the temperature fluctuations lead to loss of nutrients and deterioration of meat quality, resulting in economic losses (Ali et al., 2015). The effect of repeated freezing and thawing on muscle protein and qualities has been concerned by Zhang et al. (2020).

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Section: Correlation Analysis Of Myoglobin Color Lipid Oxidation and Protein Oxidationsupporting

confidence: 90%

Influence of bleeding on myoglobin and meat quality changes of Channel catfish muscle during freeze‐thaw cycles

Huang

Wang

Xiong

et al. 2021

J. Food Process. Preserv.

View full text Add to dashboard Cite

show abstract

“…Sayd et al (2012) investigated the sarcoplasmic proteome expression of porcine LL muscle in relation to lipid oxidation during storage and cooking. The authors utilized 2-DE and tandem MS (LC-MS/MS) for proteome characterization, while lipid oxidation was determined by the thiobarbituric acid reactive substances method.…”

Section: Oxidative Stabilitymentioning

confidence: 99%

Application of proteomics to characterize and improve color and oxidative stability of muscle foods

Joseph¹,

Nair

Suman

2015

Food Research International

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“…The description of these and other methods for assessing protein oxidation in meat samples have been reviewed by Fedorova et al ( 2014 ), Alomari et al ( 2018 ), Hawkins and Davies ( 2019 ) and Hellwig ( 2020 ). Recent redox-proteomic approaches have contributed to understanding the occurrence of protein carbonylation and its underlying mechanisms in post-mortem muscle from mammals (Sayd et al 2012 ), seafood (Lin et al 2021 ), processed meat (Malheiros 2019 ; Mitra et al 2018 ) and various biological samples (Verrastro et al 2015 ; Driessen et al 2015 ).…”

Section: Concise Update On Methodological Approachesmentioning

confidence: 99%

Protein carbonylation in food and nutrition: a concise update

2021

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Protein oxidation is a topic of indisputable scientific interest given the impact of oxidized proteins on food quality and safety. Carbonylation is regarded as one of the most notable post-translational modifications in proteins and yet, this reaction and its consequences are poorly understood. From a mechanistic perspective, primary protein carbonyls (i.e. α-aminoadipic and γ-glutamic semialdehydes) have been linked to radical-mediated oxidative stress, but recent studies emphasize the role alternative carbonylation pathways linked to the Maillard reaction. Secondary protein carbonyls are introduced in proteins via covalent linkage of lipid carbonyls (i.e. protein-bound malondialdehyde). The high reactivity of protein carbonyls in foods and other biological systems indicates the intricate chemistry of these species and urges further research to provide insight into these molecular mechanisms and pathways. In particular, protein carbonyls are involved in the formation of aberrant and dysfunctional protein aggregates, undergo further oxidation to yield carboxylic acids of biological relevance and establish interactions with other biomolecules such as oxidizing lipids and phytochemicals. From a methodological perspective, the routine dinitrophenylhydrazine (DNPH) method is criticized not only for the lack of accuracy and consistency but also authors typically perform a poor interpretation of DNPH results, which leads to misleading conclusions. From a practical perspective, the biological relevance of protein carbonyls in the field of food science and nutrition is still a topic of debate. Though the implication of carbonylation on impaired protein functionality and poor protein digestibility is generally recognized, the underlying mechanism of such connections requires further clarification. From a medical perspective, protein carbonyls are highlighted as markers of protein oxidation, oxidative stress and disease. Yet, the specific role of specific protein carbonyls in the onset of particular biological impairments needs further investigations. Recent studies indicates that regardless of the origin (in vivo or dietary) protein carbonyls may act as signalling molecules which activate not only the endogenous antioxidant defences but also implicate the immune system. The present paper concisely reviews the most recent advances in this topic to identify, when applicable, potential fields of interest for future studies.

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Early post-mortem sarcoplasmic proteome of porcine muscle related to lipid oxidation in aged and cooked meat

Cited by 17 publications

References 36 publications

Influence of bleeding on myoglobin and meat quality changes of Channel catfish muscle during freeze‐thaw cycles

Influence of bleeding on myoglobin and meat quality changes of Channel catfish muscle during freeze‐thaw cycles

Application of proteomics to characterize and improve color and oxidative stability of muscle foods

Protein carbonylation in food and nutrition: a concise update

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