Effects of hydrodynamic pressure processing and blade tenderization on intramuscular collagen and tenderness-related protein characteristics of top rounds from Brahman cattle

This study evaluated the effects of blade tenderization (BT), hydrodynamic pressure processing (HDP) and BT followed by HDP (BT + HDP) on collagen solubility and tenderness-related protein characteristics in top rounds from Brahman cattle. Top rounds (n = 12) were divided in half and randomly assigned to HDP, BT or BT + HDP with each treatment sample having a paired control. HDP and BT + HDP increased (P < 0.0001) collagen solubility, but the correlation between percent soluble collagen and tenderness was low (r = -0.41). All three treatments increased (P < 0.01) fragmentation of myofibrils 35% compared with controls. HDP and BT + HDP treatments increased (P < 0.05) the content of a 100 to 110-kDa protein observed in myofibrillar protein fractions by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). Minimal treatment differences were observed in sarcoplasmic proteins using SDS-PAGE. Results suggest BT physically disrupts the muscle structure to improve tenderness while HDP tenderization potentially results from both physical disruption of the muscle structure and some form of direct alterations to muscle proteins.