Tenderization of beef with bacterial collagenase

Area of Science:

• Food Science and Technology
• Biochemistry
• Enzymology

Background:

• Current meat tenderization methods often rely on plant-derived proteinases like papain, bromelain, and ficin.
• Investigating microbial enzymes offers potential for novel and effective meat tenderization solutions.

Purpose of the Study:

• To evaluate the feasibility of using purified collagenase from Clostridium histolyticum as a meat tenderizer.
• To compare the collagenase activity with existing plant-based proteinases in model systems.
• To assess the tenderization effect of collagenase on raw beef steaks during cooking.

Main Methods:

• Enzyme activity assays were performed in model systems to compare collagenase with papain, bromelain, and ficin.
• Collagenase activity was characterized across a temperature range (40-60°C).
• Raw beef steaks were treated with collagenase and cooked in a water bath; tenderness was assessed using Warner-Bratzler shear force analysis.

Main Results:

• Collagenase demonstrated higher activity in hydrolyzing insoluble collagen compared to salt-soluble protein (SSP).
• Optimal collagenase activity was observed between 40°C and 60°C, with minimal activity above 60°C.
• Tenderization achieved with collagenase in steaks was comparable to that of NaCl or a combination of CaCl(2), NaCl, and collagenase.

Conclusions:

• Purified Clostridium histolyticum collagenase exhibits enzymatic activity suitable for potential meat tenderization applications.
• The observed tenderization effect in meat was not significantly superior to conventional methods, possibly due to evaluation method sensitivity or meat matrix interactions.
• Further investigation is warranted to optimize collagenase application in meat processing and overcome potential limitations in the meat environment.