ISSN:
1745-4573
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Process Engineering, Biotechnology, Nutrition Technology
Notes:
Fresh bovine longissimus thoracis muscle samples, heated at 73C for 0, 5, 15, 30, 45, 60, 90 and 120 min, were subjected to sodium dodecyl sulfate polyacrylamide gel electrophoresis and western blot analysis. Titin was both aggregated into large protein masses and degraded into smaller fragments (two apparently independent processes) in fresh muscle samples heated 15 min or more at 73C. Samples removed at various points during the manufacture of a tumbled cured beef product were also subjected to electrophoresis and western blot analysis. Titin was primarily degraded into smaller polypeptide fragments during the manufacture of this product with no large titin aggregates observed. Commercially manufactured meat products, when examined by these techniques, contained both titin aggregates and degradation products. These results suggest that titin can be aggregated into large protein masses and degraded into smaller polypeptide fragments during the heating of fresh or processed meat products.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1111/j.1745-4573.1992.tb00469.x
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