QUANTITATIVE DETERMINATION OF LOW‐SALT SOLUBLE PROTEIN PATTERNS OF BOVINE MUSCLES COOKED AT DIFFERENT TEMPERATURES, BY SODIUM DODECYL SULFATE‐POLYACRYLAMIDE GEL ELECTROPHORESIS
1980; Wiley; Volume: 45; Issue: 4 Linguagem: Inglês
10.1111/j.1365-2621.1980.tb07475.x
ISSN1750-3841
AutoresHugo A. Caldironi, Nicolas G. Bazán,
Tópico(s)Meat and Animal Product Quality
ResumoABSTRACT 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.
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