New Insights in Muscle Biology that Alter Meat Quality

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Abstract

Fresh meat quality is greatly determined through biochemical changes occurring in the muscle during its conversion to meat. These changes are key to imparting a unique set of characteristics on fresh meat, including its appearance, ability to retain moisture, and texture. Skeletal muscle is an extremely heterogeneous tissue composed of different types of fibers that have distinct contractile and metabolic properties. Fiber type composition determines the overall biochemical and functional properties of the muscle tissue and, subsequently, its quality as fresh meat. Therefore, changing muscle fiber profile in living animals through genetic selection or environmental factors has the potential to modulate fresh meat quality. We provide an overview of the biochemical processes responsible for the development of meat quality attributes and an overall understanding of the strong relationship between muscle fiber profile and meat quality in different meat species.

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Integrative genomics identifies MCU as an essential component of the mitochondrial calcium uniporter.

Joshua M Baughman, Fabiana Perocchi, Hany S. Girgis … (2011)

Mitochondria from diverse organisms are capable of transporting large amounts of Ca(2+) via a ruthenium-red-sensitive, membrane-potential-dependent mechanism called the uniporter. Although the uniporter's biophysical properties have been studied extensively, its molecular composition remains elusive. We recently used comparative proteomics to identify MICU1 (also known as CBARA1), an EF-hand-containing protein that serves as a putative regulator of the uniporter. Here, we use whole-genome phylogenetic profiling, genome-wide RNA co-expression analysis and organelle-wide protein coexpression analysis to predict proteins functionally related to MICU1. All three methods converge on a novel predicted transmembrane protein, CCDC109A, that we now call 'mitochondrial calcium uniporter' (MCU). MCU forms oligomers in the mitochondrial inner membrane, physically interacts with MICU1, and resides within a large molecular weight complex. Silencing MCU in cultured cells or in vivo in mouse liver severely abrogates mitochondrial Ca(2+) uptake, whereas mitochondrial respiration and membrane potential remain fully intact. MCU has two predicted transmembrane helices, which are separated by a highly conserved linker facing the intermembrane space. Acidic residues in this linker are required for its full activity. However, an S259A point mutation retains function but confers resistance to Ru360, the most potent inhibitor of the uniporter. Our genomic, physiological, biochemical and pharmacological data firmly establish MCU as an essential component of the mitochondrial Ca(2+) uniporter.

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Mechanisms of water-holding capacity of meat: The role of postmortem biochemical and structural changes.

S Lonergan, Elisabeth Huff-Lonergan (2005)

Unacceptable water-holding capacity costs the meat industry millions of dollars annually. However, limited progress has been made toward understanding the mechanisms that underlie the development of drip or purge. It is clear that early postmortem events including rate and extent of pH decline, proteolysis and even protein oxidation are key in influencing the ability of meat to retain moisture. Much of the water in the muscle is entrapped in structures of the cell, including the intra- and extramyofibrillar spaces; therefore, key changes in the intracellular architecture of the cell influence the ability of muscle cells to retain water. As rigor progresses, the space for water to be held in the myofibrils is reduced and fluid can be forced into the extramyofibrillar spaces where it is more easily lost as drip. Lateral shrinkage of the myofibrils occurring during rigor can be transmitted to the entire cell if proteins that link myofibrils together and myofibrils to the cell membrane (such as desmin) are not degraded. Limited degradation of cytoskeletal proteins may result in increased shrinking of the overall muscle cell, which is ultimately translated into drip loss. Recent evidence suggests that degradation of key cytoskeletal proteins by calpain proteinases has a role to play in determining water-holding capacity. This review will focus on key events in muscle that influence structural changes that are associated with water-holding capacity.

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Current research in meat color.

R Mancini, Andrea Hunt (2005)

This review surveyed recent literature focused on factors that affect myoglobin chemistry, meat color, pigment redox stability, and methodology used to evaluate these properties. The appearance of meat and meat products is a complex topic involving animal genetics, ante- and postmortem conditions, fundamental muscle chemistry, and many factors related to meat processing, packaging, distribution, storage, display, and final preparation for consumption. These factors vary globally, but the variables that affect basic pigment chemistry are reasonably consistent between countries. Essential for maximizing meat color life is an understanding of the combined effects of two fundamental muscle traits, oxygen consumption and metmyoglobin reduction. In the antemortem sector of research, meat color is being related to genomic quantitative loci, numerous pre-harvest nutritional regimens, and housing and harvest environment. Our knowledge of postmortem chilling and pH effects, atmospheres used for packaging, antimicrobial interventions, and quality and safety of cooked color are now more clearly defined. The etiology of bone discoloration is now available. New color measurement methodology, especially digital imaging techniques, and improved modifications to existing methodology are now available. Nevertheless, unanswered questions regarding meat color remain. Meat scientists should continue to develop novel ways of improving muscle color and color stability while also focusing on the basic principles of myoglobin chemistry.

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Author and article information

Journal

Title: Annual Review of Animal Biosciences

Abbreviated Title: Annu. Rev. Anim. Biosci.

Publisher: Annual Reviews

ISSN (Print): 2165-8102

ISSN (Electronic): 2165-8110

Publication date Created: February 16 2021

Publication date (Print): February 16 2021

Volume: 9

Issue: 1

Pages: 355-377

Affiliations

[1 ]Animal Science Department, College of Animal Science and Food Engineering, University of São Paulo, Pirassununga, São Paulo, Brazil 13635-900;

[2 ]Department of Animal and Poultry Sciences, Virginia Polytechnic Institute and State University, Blacksburg, Virginia 24061, USA;

Article

DOI: 10.1146/annurev-animal-021419-083902

PubMed ID: 33338390

SO-VID: 89f70a30-9cd9-4095-9e77-b36e59abac8e

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New Insights in Muscle Biology that Alter Meat Quality

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Preventive and Emergency Medicine Insights

Most cited references 141

Integrative genomics identifies MCU as an essential component of the mitochondrial calcium uniporter.

Mechanisms of water-holding capacity of meat: The role of postmortem biochemical and structural changes.

Current research in meat color.

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Cited by 17

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