Extracellular modifications to muscle collagen: implications for meat quality

Area of Science:

• Muscle biology
• Biochemistry
• Food science

Background:

• The muscle extracellular matrix (EMC) is primarily collagen.
• Collagen crosslinking is crucial for EMC stability and muscle function.
• Crosslinks affect meat texture, especially during cooking.

Purpose of the Study:

• To review extracellular modifications of collagen, focusing on crosslinking.
• To discuss the impact of collagen crosslinks on muscle and meat properties.
• To explore current knowledge gaps in crosslinking regulation.

Main Methods:

• Review of existing literature on collagen crosslinking.
• Analysis of factors influencing collagen crosslinking patterns.
• Examination of the role of proteoglycans in collagen fibrillogenesis.

Main Results:

• Enzyme-mediated, lysine-derived covalent crosslinks stabilize the muscle EMC.
• Collagen and crosslink concentrations vary by muscle type, affecting texture.
• Cooking denatures collagen, increasing meat toughness due to crosslinks.
• Decorin may regulate collagen fibrillogenesis and influence crosslinking.

Conclusions:

• Collagen crosslinking is essential for muscle structure and meat quality.
• Mechanisms regulating collagen crosslink formation require further investigation.
• Proteoglycans like decorin show potential in modulating collagen organization and crosslinking.