Hostname: page-component-848d4c4894-sjtt6 Total loading time: 0 Render date: 2024-06-22T22:17:39.352Z Has data issue: false hasContentIssue false

Postmortem proteolysis in pork does not depend on fibre type distribution

Published online by Cambridge University Press:  20 November 2017

M. Christensen
Affiliation:
The Royal Veterinary and Agricultural University, Department of Dairy and Food Science, Rolighedsvej 30, DK-1958 Frederiksberg C, Denmark
P. Henckel
Affiliation:
Danish Institute of Agricultural Sciences, Department of Product Quality, Postbox 50, DK-8830 Tjele, Denmark
P.P. Purslow
Affiliation:
The Royal Veterinary and Agricultural University, Department of Dairy and Food Science, Rolighedsvej 30, DK-1958 Frederiksberg C, Denmark
Get access

Extract

Proteolytic degradation is known to be faster in white muscles than in red muscles (Whipple & Koohmaraie, 1992). Variation in eating quality between muscles has often been correlated to their metabolic properties, as determined by the fibre type distribution. Correlations between fibre type distribution and postmortem proteolysis could result from two possible effects: (1) Due to their inherent differences in metabolic potential, composition and content of proteolytic enzymes, fibres of some types may degrade more than others. (2) The balance of fibre types controls postmortem (p.m.) metabolic characteristics of the muscle as a whole, with all fibre types within it being equally affected. An experiment was conducted to compare the rate of postmortem proteolysis in five porcine muscles differing in fibre type distribution and to compare the rate of proteolysis in type II fibres isolated from these muscles.

Type
Poster Presentations
Copyright
Copyright © The British Society of Animal Science 2001

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

Brooke, M.H. and Kaiser, K.K.. 1970. Arch Neurol. 23: 369.Google Scholar
Fritz, J.D., Swartz, D.R. and Greaser, M.L.. 1989. Anal. Biochem. 180: 205.Google Scholar
Whipple, G. and Koohmaraie, M.. 1992. J. Anim. Sci. 70: 798.Google Scholar