Alterations in the sarcoplasmic protein fraction of beef muscle with postmortem aging and hydrodynamic pressure processing.

UNLABELLED

Capillary electrophoresis (CE) and reversed-phase high performance liquid chromatography (RP-HPLC) analyses were utilized to detect differences in the sarcoplasmic protein fractions of beef strip loins subjected to aging and hydrodynamic pressure processing (HDP) treatments. At 48 h postmortem, strip loins (n = 12) were halved and subjected to control or HDP treatments. Following treatment, each half was divided into 3 portions which were aged for 0, 5, and 8 d. After each aging period, steaks were removed for Warner-Bratzler shear force (WBSF) analysis and for the extraction of sarcoplasmic proteins which were analyzed by CE and RP-HPLC. Aging by HDP interactions were not detected using either separation technique. With CE analysis, no HDP effects were observed; however, the relative peak area of 8 protein peaks ranging in size from 17 to >200 kDa were influenced by postmortem aging. Separation of proteins by RP-HPLC demonstrated that HDP influenced the relative size of 2 protein peaks while postmortem aging effects were observed in 6 peaks. Alterations in the sarcoplasmic protein fractions detected by both CE and RP-HPLC were correlated to WBSF measurements. Overall, data demonstrate that HDP has minimal effects on sarcoplasmic proteins and that aging related changes in the water soluble protein fractions of muscle may be useful as indirect indicators of beef tenderness.

PRACTICAL APPLICATION

Using 2 different postmortem tenderization techniques, aging and hydrodynamic pressure processing, this study demonstrates that postmortem changes in the soluble protein fraction of beef may be useful as potential indicators of meat tenderness.