What are collagen peptides?
Collagen peptides are repair collagen, and the protein slowly decreases with age. It can be seen that collagen does play a pivotal role in the health and beauty of human skin. Collagen peptides are short-chain protein fragments that are formed by the hydrolysis process of collagen. Collagen is one of the most abundant proteins in the human body and is mainly found in skin, bones, muscles, and connective tissues. It is the smallest unit of collagen, and its structure can be expressed as (Gly-x-y), which is a high-purity peptide with glycine at the N-terminus, compared with the molecular weight of 2,000~3,000 Da of ordinary collagen, collagen peptide has a smaller molecular weight and higher bioavailability, making it easier to be absorbed and utilized by the body than original collagen.
How are collagen peptides made?
Using advanced directional enzyme digestion, denaturation, drying, extraction and other technologies, the average molecular weight of collagen peptides is about 1,000 Da, compared with the complex three-stage supercoiled structure of collagen, the linear structure of collagen peptides makes its digestion and absorption rate as high as 80% (collagen is ≤1%).
The process of making collagen peptides mainly consists of two steps: collagen extraction and hydrolysis. First, raw collagen is extracted from animal skin, bones, or fish scales. The extracted collagen is then hydrolyzed using enzymes or acids to break it down into short-chain amino acid fragments, known as collagen peptides. Different hydrolysis conditions affect the molecular weight, amino acid composition, and biological activity of collagen peptides. The resulting collagen peptide has high bioavailability due to its small molecular weight, and can be quickly absorbed and utilized by the body.
Table 1 Collagen peptides at Creative Peptides.
Types of collagen peptides
The types of collagen peptides can be classified from two main dimensions: source and molecular weight:
Source classification
Animal sources: including collagen peptides from chickens, cattle and other animals. For example, the types of collagen peptides in chickens include I, II, III, IV, VI, IX, XI, XII, XXVI, etc. The types of collagen peptides in bovines include I, II, IV, VIII, etc.
Marine sources: mainly fish collagen peptides, such as fish scales, fish skin, etc., including I, II, IV, V, VI, XII, XIV, XXVIII and other types.
Molecular weight classification
The molecular weight of collagen peptides varies according to their amino acid composition and structure, and is usually between 300-20,000 Da. The average molecular weight of hydrolyzed collagen products on the market is about 1,000 Da, and the molecular weight can be reduced to less than 500 Da through high-tech treatment.
Collagen peptides benefits
Collagen peptides have a variety of health benefits and are widely used in the fields of beauty, health and sports nutrition.
Promotes healthy skin
Collagen peptides have a particularly significant impact on skin health. As we age, collagen in the body naturally decreases, causing the skin to lose elasticity and moisture. Supplementing collagen peptides can increase skin hydration, reduce the appearance of wrinkles and fine lines, and make the skin firmer and smoother. In addition, collagen peptides can also enhance the skin barrier function, resist the damage of the external environment to the skin, and delay skin aging.
Supports intestinal health
In recent years, the benefits of collagen peptides in gut health have also gained traction. It can promote the repair of the intestinal barrier, reduce intestinal leakage, and prevent the occurrence of intestinal diseases. In addition, collagen peptides balance the gut microbiota, promote digestive health and nutrient absorption, and improve overall digestive function.
Promotes wound healing
Collagen plays a key role in wound healing. Collagen peptides can accelerate the repair of skin wounds, promote the formation of new tissues, and reduce the production of scars. This is especially important for recovery after surgery or trauma.
Improves cardiovascular health
Collagen peptides may also have benefits for cardiovascular health. Studies have shown that collagen peptides can help prevent cardiovascular disease by lowering blood pressure, improving blood vessel elasticity, and reducing the risk of arteriosclerosis. This is especially important for people at risk of cardiovascular disease.
What do collagen peptides do?
Collagen peptides exert their effects through a variety of mechanisms. First of all, specific amino acids in collagen peptides, such as glycine, proline, and hydroxyproline, are important components that make up collagen. These amino acids can be directly absorbed and utilized by skin, bone and joint tissues to promote tissue repair and regeneration. Secondly, collagen peptides are able to activate collagen synthesis in the body and stimulate the proliferation and activity of fibroblasts, thereby increasing the content of collagen in tissues. Finally, collagen peptides also have antioxidant and anti-inflammatory effects, which are able to protect cells from oxidative stress and inflammation, further promoting tissue health and function.
Collagen peptides and other collagen proteins
Collagen peptides, marine collagen, and hydrolyzed collagen are all derived from animal collagen, mainly from tissues such as skin, bone, cartilage, etc. Marine collagen is usually derived from fish skin or fish scales, while collagen peptides and hydrolyzed collagen can be derived from a variety of animal sources.
Collagen peptides vs hydrolyzed collagen
Although collagen peptides and hydrolyzed collagen can be confused in name, there is a significant difference between them. Hydrolyzed collagen is a macromolecular protein obtained by partial hydrolysis of collagen, and its molecular weight is usually between a few thousand and hundreds of thousands of daltons. In contrast, collagen peptides are short-chain peptide molecules that are hydrolyzed from collagen that has been further hydrolyzed, typically with molecular weights ranging from a few hundred to a few thousand daltons. Due to its small molecular weight, collagen peptides have higher absorption efficiency and bioavailability, allowing them to be absorbed and function more quickly by tissues in the body. As a result, collagen peptides are more popular in many health and beauty products.
Marine collagen vs collagen peptides
Marine collagen and collagen peptides are both popular health supplements, but their sources and properties differ. Marine collagen generally refers to collagen extracted from fish, specifically fish skin and scales. Because its molecular structure is more similar to that of human collagen, marine collagen excels at improving skin elasticity and improving skin texture. In addition, marine collagen is usually rich in type I collagen, which has a strong moisturizing effect.
However, marine collagen is usually present in the form of macromolecules, so it is not as efficient in absorption as collagen peptides that have been hydrolyzed. Due to their small molecular weight and excellent bioavailability, collagen peptides can be absorbed more quickly by tissues in the body, making them suitable for a wider range of health management needs. In addition, due to the problem of the source of marine collagen, some people may have an allergic reaction to it, and collagen peptides have shown a higher safety profile in this case.
Summary
Overall, collagen peptides have become an essential part of the modern health and beauty landscape due to their efficient absorption and wide range of health benefits. Whether it's for improving skin health, promoting bone strength, or improving joint mobility, collagen peptides have shown great potential. With the growing demand for health and anti-aging, the application prospect of collagen peptides will be broader.
Reference
- Czajka, Anna, et al., Daily oral supplementation with collagen peptides combined with vitamins and other bioactive compounds improves skin elasticity and has a beneficial effect on joint and general wellbeing. Nutrition Research 57 (2018): 97-108.
