Is collagen a complete protein?
ABUNDANT AMINO ACIDS
Collagen is the most abundant type of protein in your body, forming your bones, joints, cartilage, gut lining, skin, hair, and nails.
When you consume collagen-rich foods, the amino acid building blocks are used to build and maintain structural tissues.
WHY IS IT A "BEAUTY PRODUCT"?
When you have an abundance of collagen building blocks, your body can dedicate them to promoting glowing hair, skin, and nails (these standards of beauty are in fact indicators of nutrient status).
As you age, your body produces less collagen, making it an important nutrient to include in your diet (this is why collagen is often marketed as a beauty product).
THE WHOLE-FOOD FORM
Traditionally, people obtain collagen by consuming the skin, cartilage, marrow, or bone broth from animals.
These are rich (and generally inexpensive) sources of whole-food collagen that you can incorporate into your diet (that also contain many minerals).
Collagen is not a "complete protein" because it does not contain the essential amino acid tryptophan.
HYDROLYZED COLLAGEN
Hydrolyzed collagen peptides have recently entered the health food market as an easy way to boost your collagen intake.
These products are usually sourced from eggshells or the bones/skin of beef, chicken, or fish, so quality should be considered.
Collagen powder has a versatile taste and texture for incorporating into your favorite foods and beverages.
WHY ARE THERE 5 TYPES?
There are 5 types of collagen proteins: I, II, III, X, V.
Some collagen products advertise containing all 5, others contain only I and III because they are the most abundant and useful in the body.
Contrary to some marketing claims, there is no such thing as "plant-based" or "vegan collagen" because it is a protein only found in animals.
WAYS TO INCORPORATE COLLAGEN PEPTIDES
coffee
tea
soup
protein balls
oatmeal
baked goods
*Collagen powder dissolves well in hot or cold liquids.
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References
Choi, F. D., Sung, C. T., Juhasz, M. L., & Mesinkovsk, N. A. (2019). Oral Collagen Supplementation: A Systematic Review of Dermatological Applications. Journal of drugs in dermatology : JDD, 18(1), 9–16.
Frasca, G., Cardile, V., Puglia, C., Bonina, C., & Bonina, F. (2012). Gelatin tannate reduces the proinflammatory effects of lipopolysaccharide in human intestinal epithelial cells. Clinical and experimental gastroenterology, 5, 61–67. https://doi.org/10.2147/CEG.S28792
Samonina, G., Lyapina, L., Kopylova, G., Pastorova, V., V, Bakaeva, Z., Jeliaznik, N., Zuykova, S., & Ashmarin, I., I (2000). Protection of gastric mucosal integrity by gelatin and simple proline-containing peptides. Pathophysiology : the official journal of the International Society for Pathophysiology, 7(1), 69–73. https://doi.org/10.1016/s0928-4680(00)00045-6
Moskowitz R. W. (2000). Role of collagen hydrolysate in bone and joint disease. Seminars in arthritis and rheumatism, 30(2), 87–99. https://doi.org/10.1053/sarh.2000.9622
Organic Consumers. The True Content and Faces Behind America’s Best-Selling Collagen. Retreived from https://www.organicconsumers.org/sites/default/files/collagen_white_paper.pdf