ISSN:
1750-3841
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
,
Process Engineering, Biotechnology, Nutrition Technology
Notes:
Muscle samples from bovine animals were cooked for 10 min from 60–90°C with intervals of about 2°C. Samples were homogenized and centrifuged and the low-salt soluble proteins were obtained thereafter. Photodensitometry was used for the quantitation of proteins on SDS polyacrylamide gels with the enzyme enolase as an internal standard. It was found that a linear relationship existed between peak areas and the enolase concentration up to 60 μg. Enolase was found to be a useful internal standard yielding narrower bands in the middle of the gel than other tested proteins. When muscles were cooked at temperatures between 60–80°C, low-salt soluble proteins gradually disappeared and could not be detected above 80°C. From 68°C towards higher temperatures, protein bands of the following molecular weights were observed: 130,000; 85,000; 72,000; 55,000; 40,000, and 18,000. A quantitative relationship was established between the bands of 55,000 and 40,000. The ratio between these two bands went from a value higher than one to a value lower than one, at 68–72°C. Since the foot-and-mouth disease virus is inactivated at about 70°C, the present method could be applied in studies on the effectiveness of heat processing in destroying the infective virus.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1111/j.1365-2621.1980.tb07475.x
Permalink