Skip to content

Myosin: What is the main protein in meat called?

5 min read

According to food science research, myofibrillar proteins like myosin and actin make up over 50% of the total protein in meat. This is why the main protein in meat is called myosin, working in tandem with actin and other proteins to form the muscle structure we consume.

Quick Summary

Myosin is the most abundant protein in muscle fibers, and it partners with actin to facilitate muscle contraction. The composition of meat also includes other vital proteins, such as myoglobin and collagen, which influence its color, texture, and tenderness.

Key Points

  • Myosin and Actin Are Key: Myosin is the most abundant protein in muscle tissue and works with actin to enable muscle contraction.

  • Myoglobin Colors Meat: The red color of meat is primarily due to the sarcoplasmic protein myoglobin, which stores oxygen in muscle cells.

  • Collagen Affects Tenderness: Collagen is a connective tissue protein that can be broken down by low-and-slow cooking, turning into gelatin and making meat tender.

  • Different Proteins, Different Cooking Methods: Myofibrillar proteins become tougher with heat, while collagen requires heat to become tender. This is why different cuts of meat need different cooking techniques.

  • Aging Improves Tenderness: The tenderness of meat increases during the aging process as natural enzymes break down muscle proteins like troponin.

  • Connective Tissue Varies by Cut: The amount and type of connective tissue, including collagen and elastin, varies by muscle location, influencing the meat's natural tenderness.

  • Elastin Stays Tough: Unlike collagen, the connective tissue protein elastin is not broken down by cooking and remains tough, often forming the 'gristle' in meat.

In This Article

A Deeper Dive into Meat's Primary Protein: Myosin

Meat is a complex food product, and its texture, flavor, and nutritional value are all defined by its protein makeup. While many people simply think of "meat" as a source of protein, it's the specific types and their interactions that truly tell the story. Myosin is quantitatively the most important protein in muscle tissue, the very substance that becomes meat. It is the engine of muscle contraction, existing as thick filaments within muscle cells alongside the thin filaments of actin.

The Role of Myosin in Muscle Structure

Myosin, a large and asymmetric molecule, is the fundamental component of the thick filaments found in muscle myofibrils. It has a unique structure, with a long, rod-shaped tail and a globular head. It is these heads that bind to actin filaments, creating the contractile force that allows muscles to move. In uncooked meat, this arrangement of myosin and actin forms the basis of the muscle's fibrous texture. During the postmortem process, muscle stiffens into rigor mortis due to the permanent binding of actin and myosin, a state which is later softened by enzymes during the aging process.

Other Significant Proteins Found in Meat

While myosin is the main contractile protein, it is far from the only protein present. Meat proteins are broadly classified into three categories based on their solubility.

  • Myofibrillar proteins: These are the most abundant group, comprising 50–55% of the total protein. They are salt-soluble and include myosin and actin, which are responsible for the overall muscle structure and are crucial for the water-holding capacity of meat.
  • Sarcoplasmic proteins: Making up 30–34% of the total protein, these are water-soluble. The most notable sarcoplasmic protein is myoglobin, which is responsible for meat's characteristic red color. The concentration of myoglobin varies by animal and muscle activity, which is why darker meats contain more of it.
  • Connective tissue proteins (Stromal): These make up 10–15% of the protein and are largely insoluble. The most significant are collagen and elastin.
    • Collagen: This protein forms the sheaths around muscle fibers and bundles. Unlike elastin, collagen can be broken down by low-and-slow cooking methods, converting into soft gelatin and making the meat more tender.
    • Elastin: Also known as "gristle," this protein is very tough and is not broken down by cooking. It provides elasticity to ligaments and is often trimmed from meat cuts.

The Impact of Protein Types on Cooking and Tenderness

The way different proteins respond to heat and cooking has a major impact on the final eating experience. For example, the tenderness of meat is influenced by both the contractile and connective tissue proteins.

Cooking Method vs. Protein Type

Protein Type Behavior When Cooked Best Cooking Method Result on Tenderness
Myofibrillar (Myosin & Actin) Contract and toughen at temperatures above 60°C (140°F) Quick, high-heat (e.g., grilling, searing) Cooked quickly to retain moisture and limit toughness
Connective Tissue (Collagen) Melts into gelatin when cooked low and slow, typically between 71°C and 96°C (160°F and 205°F) Slow, moist-heat (e.g., braising, stewing) Tougher cuts become tender and succulent due to gelatin formation

The Science Behind Tenderness

Tenderness is a complex trait determined by multiple factors, with protein composition being a primary one. Cuts from muscles that are used frequently, like the legs and shoulders, contain more connective tissue and coarser muscle fibers, making them tougher. In contrast, muscles that are less active, such as the tenderloin, have less connective tissue and finer fibers, resulting in more tender meat.

This explains why a quick-seared tenderloin is buttery and soft, while a tough cut like beef chuck requires hours of braising to become fall-apart tender. The low-and-slow cooking of the chuck breaks down the abundant collagen, while high heat would simply toughen the myofibrillar proteins without melting the collagen.

Conclusion: More Than a Single Protein

While myosin is undeniably the main contractile protein, it is an oversimplification to say it is the only main protein in meat. Meat is a matrix of different protein types, each serving a distinct purpose in the living animal and affecting the texture and flavor of the final dish. Myosin and actin provide the primary structure and contractile ability, while collagen influences tenderness during cooking, and myoglobin dictates color. Understanding these different protein fractions allows both chefs and home cooks to appreciate the science behind preparing a perfectly tender and flavorful meal.

The Importance of Protein Variety in Meat

Understanding the various proteins in meat goes beyond mere trivia. It informs culinary techniques, explains differences in meat cuts, and highlights the factors that contribute to the meat's final taste and texture. From the powerful muscle contractions driven by myosin and actin to the gelatinous tenderness that slow-cooked collagen provides, every protein plays a crucial role. For a deeper scientific explanation, you can read more at ScienceDirect.com.

Frequently Asked Questions About Meat Protein

What are the main types of protein in meat?

Meat contains three main classes of protein: myofibrillar proteins (myosin and actin), sarcoplasmic proteins (myoglobin), and stromal or connective tissue proteins (collagen and elastin).

Why does meat get tough when overcooked?

Overcooking causes the myofibrillar proteins (myosin and actin) to contract and squeeze out moisture, making the muscle fibers tougher and drier.

What gives meat its red color?

The color of meat is primarily due to the sarcoplasmic protein myoglobin. The concentration of myoglobin determines the meat's hue, with higher concentrations leading to a darker red color.

What is the difference between collagen and elastin in meat?

Collagen is a connective tissue protein that softens and melts into gelatin when cooked slowly with moisture. Elastin, another connective tissue protein often called gristle, remains tough and chewy regardless of cooking time.

What happens to meat protein during the aging process?

During meat aging, naturally occurring enzymes begin to break down the myofibrillar proteins, particularly affecting the troponin complex. This process helps to increase the overall tenderness of the meat.

Why are some cuts of meat more tender than others?

Cuts from less-active muscles, like the tenderloin, contain finer muscle fibers and less connective tissue, making them naturally more tender. Cuts from frequently used muscles, like the shoulder, are tougher due to more connective tissue.

How does slow cooking tenderize tough cuts of meat?

Slow cooking tough cuts like pot roast breaks down the collagen in the connective tissue, converting it into soft, moisture-rich gelatin. This counteracts the toughening effect of heat on the muscle fibers.

Frequently Asked Questions

The main contractile protein in meat is myosin, which works together with actin to cause muscle movement in the living animal and forms the structural basis of the muscle tissue we consume.

The protein myoglobin, a sarcoplasmic protein, is responsible for giving meat its characteristic red color. Higher concentrations of myoglobin lead to a darker red hue.

No, cooking does not break down all meat proteins. While heat can denature myofibrillar proteins and convert collagen to gelatin, the fibrous protein elastin remains tough and chewy.

During the aging process, proteolytic enzymes naturally present in the muscle break down myofibrillar proteins. This enzymatic breakdown helps to tenderize the meat over time.

Collagen, a connective tissue protein, is very tough in its raw form. However, with slow, moist-heat cooking, it breaks down into gelatin, which makes tough cuts of meat succulent and tender.

A tenderloin is more tender because it comes from a less-used muscle that contains less connective tissue and finer muscle fibers. Beef chuck, from an active muscle, has more connective tissue and coarser fibers, making it tougher.

Meat proteins are categorized into three groups based on their solubility: myofibrillar (e.g., myosin, actin), sarcoplasmic (e.g., myoglobin), and stromal or connective tissue proteins (e.g., collagen, elastin).

References

  1. 1
  2. 2
  3. 3
  4. 4
  5. 5

Medical Disclaimer

This content is for informational purposes only and should not replace professional medical advice.