2012
DOI: 10.1016/j.meatsci.2012.03.013
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Advances in apoptotic mediated proteolysis in meat tenderisation

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Cited by 149 publications
(101 citation statements)
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“…The proteome changes during the muscle-to-meat conversion process are radical; many studies have been finalized to shed light on these variations [36], [37], [38], [39] and [40], and many others demonstrated the process of muscle proteolysis as the hub of muscle evolution into meat [41], [42] and [43]; our 2D results are in agreement with previous findings, as stated by variations in differential spots containing structural proteins: spots 458, 459, 466 and 471 are identified as troponin T. The time course trend indicates that an important downregulation of troponin T of longissimus thoracis Piedmontese muscle begins to appear from day 17 onward, to reach its top at day 44 (4.3 fold change for spot 458; 7.2 fold change for spot 459, Table 1); this experimental result rewards the 44 days-aged meat, because, as it has been previously reported [38] and [44], degradation of troponin T is known to be a descriptive indicator of meat tenderization process. Another component of muscular architecture, actin, clearly describes the ongoing proteolysis during the aging period; later in our discussion we will recall the upward trend of a particular actin fragment (31 kDa) linked with apoptosis.…”
Section: Proteolysismentioning
confidence: 99%
“…The proteome changes during the muscle-to-meat conversion process are radical; many studies have been finalized to shed light on these variations [36], [37], [38], [39] and [40], and many others demonstrated the process of muscle proteolysis as the hub of muscle evolution into meat [41], [42] and [43]; our 2D results are in agreement with previous findings, as stated by variations in differential spots containing structural proteins: spots 458, 459, 466 and 471 are identified as troponin T. The time course trend indicates that an important downregulation of troponin T of longissimus thoracis Piedmontese muscle begins to appear from day 17 onward, to reach its top at day 44 (4.3 fold change for spot 458; 7.2 fold change for spot 459, Table 1); this experimental result rewards the 44 days-aged meat, because, as it has been previously reported [38] and [44], degradation of troponin T is known to be a descriptive indicator of meat tenderization process. Another component of muscular architecture, actin, clearly describes the ongoing proteolysis during the aging period; later in our discussion we will recall the upward trend of a particular actin fragment (31 kDa) linked with apoptosis.…”
Section: Proteolysismentioning
confidence: 99%
“…Nonetheless, there is no technique that is used in the current system to predict meat tenderness of a carcass precisely at abattoir level to classify tenderness according to eating quality. Meat tenderness is highly variable and is affected by the meat cut and a range of intrinsic and extrinsic factors associated with the conversion of muscle to meat (Kemp & Parr, 2012;García-Marcia et al, 2014;Guzek et al, 2016). Zhao et al (2014) stated that beef tenderness is a complex trait that can further be dictated by the four structural elements of the muscle (muscle fibres, sarcomere length, connective tissue, and intramuscular fat) Swatland (2003) highlighted the challenge to improve tenderness through genetics if nanostructure components, such as sarcomere length, muscle fibre orientation, and fibre texture, are not known.…”
Section: Tenderness and Fat Content Evaluation In The Current System mentioning
confidence: 99%
“…However, tenderisation mainly results from proteolysis by the protease systems present in the muscles which are responsible for the breakdown of the protein structure. There are four systems identified thus far which include calpains, cathepsins, proteasomes and caspases (Kemp and Parr 2012). Of these systems, the calpains and cathepsins are the two which have been studied most extensively and their involvement in tenderisation have been recognised widely (Ouali 1992).…”
Section: Traditional Ageing Of Wildfowlmentioning
confidence: 99%