Tenderness--an enzymatic view. | Semantic Scholar (2025)

The use of vitamin D3 is an application tool determining tenderness improvement of beef with substantial reduction in processing costs and shorter post mortem ageing process will exceed the retail display time, which will consequently reduce losses due to unsold meat being returned from shops to the manufacturers.

This document summarizes current capabilities, research and operational priorities, and plans for further studies that were established at the 2015 USGS workshop on quantitative hazard assessments of earthquake-triggered landsliding and liquefaction in the Central American region.

The role of CAPN1, calpain II (CAPN2) and CAST in post-mortem meat tenderization, and the relationship between CAPN3 and tenderness in domestic animals are summarized and analysed.

There was a relationship between length polymorphisms of CA repeat located 5’ to the promoter region of Type I bovine cal Pastatin which altered the level of calpastatin transcripts and ultimately influenced meat shear force value due to the variation in calpain inhibition.

The characterization of calpains is described as well as describes the construction and functioning of the system ofCalpains, which plays a major role in postmortem proteolysis and meat tenderization.

The effect of temperature and time of post-mortem delay in rat and dog tissues for some commonly used cellular markers: cytokeratin, vimentin, factor VIII-related antigen, Ki67, PCNA and activated caspase 3 is illustrated using previously unpublished data from a number of studies.

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How calpain activity is regulated in cells is still unclear, but the calpains ostensibly participate in a variety of cellular processes including remodeling of cytoskeletal/membrane attachments, different signal transduction pathways, and apoptosis.

A differential response of the two muscle types to mildly elevated plasma epinephrine concentration and the response to elevated epinphrine may be at the translational or posttranslational level are indicated.

This work has shown that apoptotic cell death is a genetically programmed, morphologically distinct form of cell death that can be triggered by a variety of physiological and pathological stimuli, and that proteases play critical roles in initiation and execution of this process.

There was no direct evidence from this study that caspases have a significant role in postmortem tenderization, but they may have some role through calpastatin degradation.

This crystal structure of the calcium-bound calpain 2 heterodimer bound by one of the four inhibitory domains of calpastatin is reported, which reveals the conformational changes that calpain undergoes on binding calcium, which include opening of the active site cleft and movement of the domains relative to each other to produce a more compact enzyme.

Two crystal structures show how an inhibitory protein domain gags one such enzyme without being chewed up itself.

The 3.0 Å structure of Ca2+-bound m-calpain in complex with the first calpastatin repeat, both from rat, is reported, revealing the mechanism of exclusive specificity and highlighting the complexity of calpain activation by Ca2+, illustrating key residues in a peripheral domain that serve to stabilize the protease core onCa2+ binding.

Functional characterization of CAST variation should enhance understanding of the molecular basis of pork tenderness, and thus allow for genetic improvement of pork products.

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