Tenderization of beef with bacterial collagenase.

The feasibility of using a purified collagenase produced by Clostridium histolyticum as a meat tenderizer was studied. Experiments were conducted with enzymes in model systems to compare collagenase with the currently used plant proteinases, papain, bromelain and ficin. Collagenase was shown to have a greater activity in hydrolyzing insoluble collagen than salt-soluble-protein (SSP) and highest activity between 40° and 60°C, with little to no activity above 60°C. Collagenase was added to raw steaks and steaks were placed in bags and cooked in a water bath to 6.5°C. Tenderness was evaluated by analyzing components of Warner-Bratzler shear-deformation curves. The results suggested that addition of NaCl or a combination of CaCl(2), NaCl and collagenase would cause equivalent tenderization. The lack of a significant tenderization due to collagenase could be related to a lack of sensitivity in the shear evaluation or an effect on the enzyme activity due to the meat environment.