ISSN:
1750-3841
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
,
Process Engineering, Biotechnology, Nutrition Technology
Notes:
: In order to determine the involvement of μ-calpain in the tenderization of meat during postmortem aging, μ-calpain was prepared from porcine skeletal muscle and its activity was measured under various conditions, using casein and myofibrils as the substrate. μ-Calpain was inactive at pH 5.89 and below 15 °C. Even when the reaction time was extended to 10 h, it was entirely inactive at pH 5.62 and 5 °C. In the early postmortem stage, when the pH value of muscle is above 6.0, μ-calpain was considered to be inactive due to the low concentration of sarcoplasmic calcium ions. μ-Calpain is, therefore, irrelevant to the tenderization of meat throughout postmortem aging.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1111/j.1365-2621.2002.tb10651.x
