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Proteomics, as a significant and potent postgenomic tool in the field of meat science, allows researchers to decipher underlying molecular mechanisms behind different meat quality traits. In recent years, growing attention has been paid to biomarkers accounting for meat quality attributes by means of potent proteomic technologies with the objective to gain deeper insight. This review will focus on the biomarkers of protein changes associated with the most important meat quality traits, including tenderness, color, and water-holding capacity. Molecular understanding of meat quality through application of proteomics will be conducive to generating a large amount of scientific knowledge that helps improve our understanding of meat quality, improve control, and tailor better meat quality. [ABSTRACT FROM PUBLISHER]

Searching for potential predictors of meat color is a challenging task for the meat industry. In this study, the relationship between meat color parameters and the sarcoplasmic proteome of M. longissimuss lumborum (LL) and M. psoas major (PM) from Chinese Luxi yellow cattle during post-mortem storage (0, 5, 10 and 15 days) were explored with the aid of the integrated proteomics and bioinformatics approaches. Meat color attributes revealed that LL displayed better color stability than PM during storage. Furthermore, sarcoplasmic proteins of these two muscles were compared between days 5, 10, 15 and day 0. Several proteins were closely correlated with meat color attributes and they were muscle-specific and responsible for the meat color stability at different storage periods. Glycerol-3-phosphate dehydrogenase, fructose-bisphosphate aldolase A isoform, glycogen phosphorylase, peroxiredoxin-2, phosphoglucomutase-1, superoxide dismutase [Cu–Zn], heat shock cognate protein (71 kDa) might serve as the candidate predictors of meat color stability during post-mortem storage. In addition, bioinformatics analyses indicated that more proteins were involved in glycolytic metabolism of LL, which contributed to better meat color stability of LL than PM. The present results could provide a proteomic insight into muscle-specific meat color stability of Chinese Luxi yellow cattle during post-mortem storage. [ABSTRACT FROM AUTHOR]

In the present work, changes in lipid and protein oxidation, non-heme iron (NHI) content, color and texture parameters during refrigerated storage (7 days/4 °C) of ohmically (OH) and water bath (WB)-cooked pork meat were studied. A significant effect of refrigerated storage duration and cooking method on color, texture, lipid oxidation and carbonyl content was detected for OH-cooked and WB-cooked meat. The OH-cooked meat had better color appearance, lipid oxidative stability, slightly enhanced hardness and protein oxidation levels during 7 days of storage having lower values of TBARS, center lightness ( L ⁎ ), center/surface brownness ( b ⁎ ) and free thiol groups; however, there were higher values of center/surface redness ( a ⁎ ), non-heme iron, protein carbonyl and hardness compared to those from WB-cooked meat. Industrial relevance The conventional cooking protocols always result in quality deteriorations and reduced shelf-life in meat products due to longer cooking times. In this study, the ohmically-cooked meat showed comparable or improved oxidation levels, color appearance and texture attributes during 7 days of refrigerated storage. From an anti-oxidation perspective, the available data are provided for the application of ohmic cooking in Chinese commercial productions of cooked meat with high quality requirements that could be established. [ABSTRACT FROM AUTHOR]

Abstract: The objective of this study was to investigate the effects of ohmic (OH) and waterbath (WB) cooking on colour attributes and sarcoplasmic changes of porcine longissimus dorsi muscle at the same endpoint temperatures (EPTs; range 10°C–80°C). The OH treatment was carried out at 10Vcm−1, and the WB temperature at 85°C. The colour parameters, deoxymyoglobin% (DeoMb) and metmyoglobin% (MetMb) of the OH-cooked meat were significantly lower (P <0.05) than those obtained by WB-cooking at the same EPTs (range 60°C–80°C). SDS-PAGE analysis showed that the meat treated with WB-cooking had a lower sarcoplasmic protein solubility (5.97mg/g vs.14.89mg/g, P <0.05) and fainter protein bands than that of OH-cooking thus, indicating paler colour, and lower water-holding capacity especially in WB-cooked meat at EPTs above 40°C. Strong correlations among lightness, browness, metmyoglobin% and soluble proteins were observed in meat following OH-cooking. [Copyright &y& Elsevier]