Myosin light chain 1 release from myofibrillar fraction during postmortem aging is a potential indicator of proteolysis and tenderness of beef |
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Authors: | Anderson M J Lonergan S M Huff-Lonergan E |
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Affiliation: | Department of Animal Science, Iowa State University, Ames, IA 50011 USA |
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Abstract: | 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. |
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Keywords: | Myosin light chain 1 μ-Calpain Proteolysis |
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