Protein denaturation and water‐holding capacity in pork muscle
- 1 September 1969
- journal article
- Published by Oxford University Press (OUP) in International Journal of Food Science & Technology
- Vol. 4 (3) , 269-273
- https://doi.org/10.1111/j.1365-2621.1969.tb01522.x
Abstract
Summary. The water‐holding capacity of the myofibrils from longissimus dorsi muscles of Large White pigs, selected on the basis of their rate of fall in pH post‐mortem, has been compared with the ultimate pH, the protein extractability in M potassium chloride and the adenosine triphosphatase (ATPase) activities. It was found that any loss in water‐holding capacity of the myofibrils could be attributed, mainly, to the extent of denaturation, occurring in the myofibrillar protein, as a result of a rapid fall in pH postmortem. It was also found that the ultimate pH had a small, but significant, influence on the water holding capacity.Keywords
This publication has 9 references indexed in Scilit:
- The effect of post‐mortem conditions on the extractability and adenosine triphosphatase activity of myofibrillar proteins of rabbit muscleInternational Journal of Food Science & Technology, 1967
- Quality characteristics of pork with special reference to Pietrain, Pietrain X Landrace and Landrace pigs at different weightsInternational Journal of Food Science & Technology, 1967
- The influence of pH and temperature on the properties of myosinBiochemical Journal, 1967
- The influence of post-mortem conditions on the solubilities of muscle proteinsBiochemical Journal, 1964
- Etiological Status and Associated Studies of Pale, Soft, Exudative Porcine MusculaturePublished by Elsevier ,1964
- A comparison of freeze-dried beef muscles of high or low ultimate pHJournal of the Science of Food and Agriculture, 1963
- Some Properties of the Fibrillar Proteins of Normal and Watery Pork MuscleJournal of Food Science, 1962
- Biochemistry Of Meat HydrationPublished by Elsevier ,1961
- A study of the effects of substrate concentration and certain relaxing factors on the magnesium-activated myofibrillar adenosine triphosphataseBiochemical Journal, 1956