A comparative study of the effects of high pressure on proteolytic degradation of sardine and blue whiting muscle
Article first published online: 3 AUG 2008
© 2008 Japanese Society of Fisheries Science
Volume 74, Issue 4, pages 899–910, August 2008
How to Cite
HERNÁNDEZ-ANDRÉS, A., PÉREZ-MATEOS, M., MONTERO, P. and GÓMEZ-GUILLÉN, M. D. C. (2008), A comparative study of the effects of high pressure on proteolytic degradation of sardine and blue whiting muscle. Fisheries Science, 74: 899–910. doi: 10.1111/j.1444-2906.2008.01605.x
- Issue published online: 3 AUG 2008
- Article first published online: 3 AUG 2008
- Received 28 March 2007. Accepted 10 January 2008.
- high pressure;
- myofibrillar proteins;
- proteolytic activity
ABSTRACT: High-pressure technology is used as an alternative to heat processing because of its inactivating effect on microorganisms and enzymes. However, it can also alter the structure of other muscle proteins. The present study compares the effects of high pressure (300 MPa, 7°C, 20 min) on the proteolytic degradation and alterations in the myofibrillar proteins of sardine and blue whiting muscle. Also, muscle homogenates and enzyme extracts were pressurized in order to evaluate the high-pressure effects on unprotected proteolytic enzymes outside the whole muscle structure. Peak proteolytic activity was found to occur at 55°C in both species. The peak activity pH was pH 3 for the sardine and pH 8 for the blue whiting; the main enzyme families being aspartic proteases in the former and alkaline serine proteases in the latter. Pressurization lowered activity levels at the peak activity pH and temperature in the fish muscle (by 30.8% in the sardine and by 9.5% in the blue whiting) and also slightly in the enzyme extracts (by 16.8% in the sardine and by 19.4% in the blue whiting). The electrophoretic profiles disclosed higher protein degradation in the pressurized muscle. Overall, the observed changes in proteolytic activity can be attributed not only to the effect of high pressure on the enzymes, but also and mainly, to the effect on other muscle proteins.