Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2450242 | Meat Science | 2012 | 7 Pages |
The objective of this study was to identify proteins in bovine longissimus dorsi muscle that are related to tenderness. Two dimensional difference in gel electrophoresis (2D-DIGE) was used to compare the sarcoplasmic fractions from steaks that differed in star probe values at 14 days postmortem. The intensity of myosin light chain 1 (MLC1) was greater in the sarcoplasmic fraction prepared from steaks that had lower star probe values. It was hypothesized that μ-calpain catalyzes the release MLC1 into the sarcoplasmic fraction. Myofibrils from beef longissimus dorsi were purified and incubated with μ-calpain and the appropriate buffer controls. μ-Calpain was added at 1.23 μg (0.0875 U) of pure μ-calpain/mg myofibrillar protein. Incubations of one and 120 min had a greater abundance of MLC1 in the supernatants than the control incubations. As a consequence of μ-calpain proteolysis, MLC1 is rapidly released from the myofibril and is a potential indicator of proteolysis and improvement in beef tenderness.
► Proteomic techniques are useful in identifying proteins to predict tenderization rate. ► Myosin Light Chain1 is released into the sarcoplasm early in tender beef. ► Myosin Light Chain 1 is a candidate for predicting early tenderization of beef.