Question:
Which biochemical process is responsible for aging of meat and improving the tenderness?
Which biochemical process is responsible for aging of meat and improving the tenderness?
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The calpain enzyme system targets the structural myofibrillar proteins that hold muscle fibers together. Disrupting these structural linkages makes the meat physically easier to chew.
Updated On: Jun 30, 2026
- Collagen breakdown
- Proteolytic enzyme activity
- Fat oxidation
- Moisture loss
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The Correct Option is B
Solution and Explanation
Step 1: Understanding the Question:
The question asks to identify the core biochemical process responsible for improving the tenderness of meat during post-mortem cold storage (aging).
Step 2: Detailed Explanation:
• Meat Aging: Holding carcasses or cuts of meat at refrigerated temperatures ($1^\circ\text{C} - 4^\circ\text{C}$) for several days to weeks is a standard industry practice to improve tenderness and flavor profile.
• Role of Endogenous Proteases: Post-mortem tenderization is primarily driven by the action of natural intracellular proteolytic enzymes (proteases) that break down structural proteins within muscle fibers.
• Enzyme Systems Involved:
• Calpains: Calcium-dependent neutral proteases located within the cytoplasm. They degrade key structural proteins of the myofibril, such as desmin, titin, nebulin, and troponin-T, weakening muscle fiber integrity.
• Cathepsins: Lysosomal enzymes released post-mortem as cell membranes break down, assisting in general protein degradation.
• Why Other Options are Incorrect:
• Collagen Breakdown: Collagen (connective tissue) is highly resistant to calpains. It is denatured and softened during slow, moist cooking processes (converting into gelatin) rather than during cold aging.
• Fat Oxidation: Alters the flavor profile (and causes rancidity if excessive) but does not tenderize muscle fibers.
• Moisture Loss: Occurs during dry aging, concentrating flavor, but does not biochemically tenderize the protein structure.
Step 3: Final Answer:
Endogenous proteolytic enzyme activity is the primary biochemical mechanism behind meat tenderization during aging, corresponding to option (B).
The question asks to identify the core biochemical process responsible for improving the tenderness of meat during post-mortem cold storage (aging).
Step 2: Detailed Explanation:
• Meat Aging: Holding carcasses or cuts of meat at refrigerated temperatures ($1^\circ\text{C} - 4^\circ\text{C}$) for several days to weeks is a standard industry practice to improve tenderness and flavor profile.
• Role of Endogenous Proteases: Post-mortem tenderization is primarily driven by the action of natural intracellular proteolytic enzymes (proteases) that break down structural proteins within muscle fibers.
• Enzyme Systems Involved:
• Calpains: Calcium-dependent neutral proteases located within the cytoplasm. They degrade key structural proteins of the myofibril, such as desmin, titin, nebulin, and troponin-T, weakening muscle fiber integrity.
• Cathepsins: Lysosomal enzymes released post-mortem as cell membranes break down, assisting in general protein degradation.
• Why Other Options are Incorrect:
• Collagen Breakdown: Collagen (connective tissue) is highly resistant to calpains. It is denatured and softened during slow, moist cooking processes (converting into gelatin) rather than during cold aging.
• Fat Oxidation: Alters the flavor profile (and causes rancidity if excessive) but does not tenderize muscle fibers.
• Moisture Loss: Occurs during dry aging, concentrating flavor, but does not biochemically tenderize the protein structure.
Step 3: Final Answer:
Endogenous proteolytic enzyme activity is the primary biochemical mechanism behind meat tenderization during aging, corresponding to option (B).
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