Abstract

Proteome analysis was used to investigate the relation between changes in postmortem proteome of porcine muscle and tenderness development. Muscle samples were taken at slaughter and 72 h postmortem, and the registered changes in the proteome were related to Warner-Bratzler shear force. One hundred and three protein spots were found to change significantly (P < 0.01) over time, and of these the 27 most pronounced changes were identified. Eleven out of the 27 changes were fragments of actin. Other identified myofibril proteins or fragments included myosin heavy chain, titin, myosin light chain 1, myosin light 11, CapZ, and cofilin. Correlation analysis revealed significant correlations between three of the identified actin fragments and the myosin heavy chain fragment to shear force. Moreover, myosin light chain 11 and triose phosphate isomerase I were also found to correlate significantly to shear force. The results clearly demonstrate that postmortem degradation of actin and myosin heavy chain is related to meat tenderness.

Keywords

proteome analysis; pork; porcine muscle; tenderization; two-dimensional gel electrophoresis; 2DE; matrix-assisted laser desorption/ionization time-of-flight mass spectrometry; MALDI-TOF MS; peptide-mass mapping; protein identification; shear force; Warner-Bratzler; M. longissimus dorsi

Published in

Journal of Agricultural and Food Chemistry
2003, Volume: 51, number: 24, pages: 6992-6997
Publisher: AMER CHEMICAL SOC

UKÄ Subject classification

Food Science


Publication identifier

DOI: https://doi.org/10.1021/jf034083p

Permanent link to this page (URI)

https://res.slu.se/id/publ/85635