What is Keratin and Why Is It So Strong?
Keratin is a family of fibrous structural proteins that form the primary material of hair, nails, and the outer layer of skin in humans and other animals. This protein is renowned for its durability, a characteristic that arises from its complex molecular structure. The high resilience of keratin is attributed to several key features:
- Extensive Disulfide Bonds: The amino acid cysteine is a major component of hard keratins found in hair and nails. The sulfur atoms in cysteine residues form strong disulfide bonds, creating cross-links that reinforce the protein structure and make it highly resistant to mechanical stress and chemical degradation.
- Insolubility: The tight packing of protein chains and the numerous disulfide bonds make keratin insoluble in water and most organic solvents. This insolubility is a major hurdle for our digestive enzymes, which require soluble or small-particle substrates to function effectively.
- Fibrous Structure: Keratin proteins aggregate into robust intermediate filaments, a cable-like structure that gives hair and nails their physical toughness. This dense, fibrous form is not conducive to enzymatic attack within the human digestive system.
The Human Digestive System's Inability to Process Keratin
Our digestive tract is a marvel of efficiency, equipped to break down most types of proteins, carbohydrates, and fats into usable components. However, this ability does not extend to keratin. The primary reasons for this are rooted in our biological makeup and the sheer recalcitrance of the keratin molecule.
1. Absence of Keratinase Enzymes Enzymes are the body's workhorses for digestion, with specific enzymes (proteases) targeting specific proteins. While humans produce powerful proteases like pepsin and trypsin, these enzymes are not equipped to handle the unique structure of keratin. The class of enzymes that can break down keratin is called keratinase, and it is not found in humans. Keratinase is a specialized enzyme produced by certain bacteria, fungi, and insects.
2. Resistance to Stomach Acid and Proteases Keratin's formidable structure, bolstered by disulfide bonds, makes it highly resistant to the acidic environment of the stomach and the actions of our digestive proteases. Even the strong hydrochloric acid in the stomach cannot effectively unravel the tightly wound protein structure.
3. Inaccessibility of Peptide Bonds Human proteases act by cleaving the peptide bonds within protein chains. In order for this to happen, the enzyme must be able to physically access these bonds. The compact, cross-linked structure of keratin prevents our proteases from reaching and breaking the peptide bonds, leaving the protein intact.
Comparison: Keratin vs. Other Proteins We Digest
To better understand why keratin is indigestible, it's useful to compare its properties with those of a common, easily digested protein, such as casein from milk.
| Feature | Keratin (Hair, Nails) | Casein (Milk) |
|---|---|---|
| Protein Structure | Fibrous, highly cross-linked with disulfide bonds. | Globular, with a less defined, more open structure. |
| Solubility | Insoluble in water and digestive fluids. | Soluble and readily disperses in digestive fluids. |
| Enzyme Requirement | Requires specialized keratinase enzymes, which humans lack. | Easily hydrolyzed by common human proteases like pepsin. |
| Digestibility in Humans | Indigestible; passes through the digestive tract largely intact. | Highly digestible; broken down into amino acids for absorption. |
| Formation of Obstruction | Can clump together to form bezoars, causing blockages. | Does not cause blockages; efficiently broken down into nutrients. |
The Role of Keratin in Nature and the Risks of Ingestion
While humans are unable to digest keratin, a small number of specialized organisms, such as certain bacteria, fungi, and insects, have evolved the ability to do so. These organisms, including clothes moths, some beetles, and specific bacterial species like Bacillus, produce keratinase enzymes that can break down keratinous materials like wool, feathers, and hair. This is a crucial function in the natural decomposition cycle.
For humans, accidentally swallowing a small strand of hair is usually harmless, as it will simply pass through the digestive system. However, consuming large amounts of keratinous materials, such as hair, over time can be dangerous. The indigestible matter can accumulate in the stomach or intestines and form a dense mass called a trichobezoar, or hairball. This can lead to serious health complications, including nausea, pain, and life-threatening bowel obstruction that requires medical intervention.
The Fate of Indigestible Keratin
What happens to the keratin we ingest? The journey is uneventful from a digestive standpoint.
- Ingestion: Hair or other keratinous material enters the mouth and is swallowed.
- Stomach: The material passes into the stomach. The highly acidic environment and the protease pepsin have little to no effect on the strong keratin structure.
- Small Intestine: The material continues to the small intestine. The more alkaline environment and additional proteases like trypsin and chymotrypsin also fail to break down the insoluble keratin.
- Colon: As the material moves to the large intestine, most water is absorbed, and the indigestible matter becomes part of the feces.
- Excretion: The keratin is eventually eliminated from the body as waste, having provided no nutrients in its transit.
Conclusion: We Are Not Built for Keratin
In conclusion, humans cannot digest keratin because we lack the necessary enzymes and the protein's complex, insoluble structure resists our digestive processes. This biological limitation means that hard keratin from hair, nails, and other sources passes through our bodies undigested. While minor ingestion is harmless, significant consumption poses a real risk of intestinal obstruction. While some microorganisms and other animals possess the biological machinery to degrade this tough protein, our digestive system is simply not built for the job.
Microbial production of keratinase from Bacillus velezensis strain MAMA is a great example of organisms that can break down keratin effectively.