Elucidating the Role of Apoptosis in Meat Tenderization Using the Callipyge Lamb Model
Author(s) -
T. Cramer,
M. Penick,
Jolena Waddell,
Y. H. B. Kim
Publication year - 2017
Publication title -
meat and muscle biology
Language(s) - English
Resource type - Journals
ISSN - 2575-985X
DOI - 10.22175/rmc2016.145
Subject(s) - calpastatin , tenderness , apoptosis , meat tenderness , calpain , chemistry , cytochrome c , caspase 3 , myofibril , andrology , microbiology and biotechnology , food science , biochemistry , programmed cell death , enzyme , biology , medicine
Apoptosis is the process of mediated cell death occurring immediately after exsanguination of animals. It is initiated by release of cytochrome C to the cytoplasm, ultimately activating caspase 3. Since caspase 3 is an enzyme that cleaves calpastatin, a known inhibitor of calpain (primary proteolytic enzyme), a potential involvement of apoptosis in meat tenderness development has been proposed. Previously, we presented that a higher activity of heat shock protein (HSP) 27, which has an anti-apoptotic function, and greater toughness were found in callipyge lamb loins compared with normal lamb loins. Therefore, in this study, we aimed to further investigate the role of apoptosis in the postmortem meat tenderization process using the callipyge lamb model.
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