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“Muscle to meat” molecular events and technological transformations: The proteomics insight

Cellular death is characterized by a complex pattern of molecular events that depend on cell type. Specifically, muscle cells first undergo rigor mortis due to ATP depletion, and later, on the time scale of days, muscle fiber degradation due to proteolytic enzyme activity. In the present review, we...

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Bibliographic Details
Published in:Journal of proteomics 2012-07, Vol.75 (14), p.4275-4289
Main Authors: Paredi, Gianluca, Raboni, Samanta, Bendixen, Emøke, de Almeida, André M., Mozzarelli, Andrea
Format: Article
Language:English
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Summary:Cellular death is characterized by a complex pattern of molecular events that depend on cell type. Specifically, muscle cells first undergo rigor mortis due to ATP depletion, and later, on the time scale of days, muscle fiber degradation due to proteolytic enzyme activity. In the present review, we will refer to proteomic investigations on the post-mortem evolution of the protein patterns of animal muscle cells. These studies, carried out with the application of either bottom-up or top-down methods, are relevant for understanding the biochemical reactions that i) convert muscle to meat, ii) are associated with meat aging and iii) impact on meat tenderness, a feature of significant commercial value. We also report on the proteomic investigations that have been made to analyze the transformation of meat in industrial processes. These studies are primarily aimed at identifying protein patterns and/or individual proteins diagnostic of the quality of the final product. This article is part of a Special Issue entitled: Farm animal proteomics. [Display omitted] ► Proteomics has characterized the conversion from muscle to meat in farm animals. ► Proteomics has provided insight on the molecular events associated with meat aging. ► Proteomics has defined correlations of genetic and other factors on meat tenderness. ► Proteomics identifies protein patterns diagnostic of the quality of meat products.
ISSN:1874-3919
DOI:10.1016/j.jprot.2012.04.011