Pure collagen has been promoted as a superfood.

Pure collagen has been promoted as a superfood.

Pure collagen has been promoted as a superfood. 

Claims include everything from healthy skin and nails to improvements in weight loss, muscle, and gut function.

These potential benefits make it a popular supplement among exercise and health enthusiasts.

This article examines what pure collagen is, the research behind it, and whether or not you should incorporate it into your diet. 

What is Pure Collagen

Collagen is a protein found surrounding body cells. It protects and keeps them strong [R]. 

Pure collagen is high-quality collagen that comes from grass-fed cowhide.

Predominately found in connective tissue, collagen is the most abundant protein making up 25-35 percent total body protein [R, R]. 

Collagen is also found in bone, tendons, cartilage, teeth, corneas, blood vessels, gut, and vertebral discs. 

It makes up two percent of muscle tissue and six percent of the weight of tendons [R].

Types of Pure Collagen

There are 16 types of collagen, but 80 to 90 percent of the body’s collagen consists of three types of collagen: Type I Type II and Type III. Type IV and X are two other types of collagen that are needed by the body. 

  • Type I is the most abundant collagen found in humans. It makes up the fibers of connective tissues in the skin, bone, teeth, tendons, and ligaments. It also strengthens the integrity of these tissues. [R, R].
  • Type II is found in cartilage and promotes joint health  [R]
  • Type III forms the connective tissues that give shape and strength to organs like the liver, heart, and kidneys. It promotes elasticity improving skin health [R]
  • Type IV forms sheets that lie between the layers of cells in the blood vessels, muscles, and eye. This type is necessary for the growth of the placenta and is needed during pregnancy [R]
  • Type X is collagen found in cartilage. It is needed for bone growth and health [R]

Nutrients in Pure Collagen

Amino acids are the building blocks of protein. Consuming collagen can give your body the nutrients it needs to make protein [R].  Collagen contains the following amino acids: 


Proline is the second-largest amino acid in collagen [R]. With help from vitamin C proline removes plaque [R]. It was also found to improve joint and cardiovascular health [R].


Glycine makes up about one-third of the protein found in collagen. It is what gives collagen its structure. Glycine is also responsible for lowering stress. It regulates blood vessels and improves metabolic syndrome [R, R]. 

Glycine improves skin, forms cartilage and helps with memory [R, R, R]. Glycine helps create creatine, the substance that gives muscles their power, energy and the ability to contract [R, R, R, R]. Glycine is also needed to make the antioxidant glutamine [R]. 


Glutamine is found in many body cells. When glutamine stores in the muscles are low it must be derived from the diet [R]. When there is adequate glutamine present, improvements in immune function, gut health, anxiety, concentration, and sleep have been seen [R, R, R, R, R]. Glutamine may also reduce sore muscles and fatigue [R].


Arginine regulates protein metabolism and increases oxygen circulation. This leads to muscle growth and improvements in heart health [R, R]. Arginine also supports immune [R, R].


Leucine is an essential amino acid. This means it is not made by the body and needs to be obtained from the diet [R, R]. Leucine contributes to the creation of muscle and bone. It also regulates blood glucose and helps the brain function optimally [R]. Leucine prevents muscle protein from being broken down after trauma or severe stress [R]. 


Glutamine is an antioxidant that helps to maintain a healthy gut and immune system [R]. It is also necessary for recovery after exercise. Glutamine helps to rebuild damaged muscle [R].


Lysine must be obtained from the diet and is needed for growth and repair. Large amounts are found in the muscles. Lysine is what helps form collagen fibers. It promotes calcium metabolism. Lysine helps create carnitine, a compound that gives the muscles energy. Lysine helps produce healthy bones and improves immune function [R].


Hydroxylysine another main component of collagen [R]. It is responsible for skin, joint, tendon, and cartilage health [R, R].


Hydroxyproline is similar to proline and a main component of collagen. It makes up bone and connective tissue [R].


Histidine must be obtained from the diet. It helps to maintain iron levels [R].


Alanine helps the liver generate energy [R].


Isoleucine must be obtained from the diet [R].


Tyrosine is mostly found in the muscles. It regulates the nervous system and helps with brain function [R].


Valine must be obtained from the diet. It fuels muscles with energy, stimulates the nervous system, and helps improve brain function [R, R, R].

What Does Pure Collagen Do

Collagen gets its name from the Greek word κόλλα which means glue. Collagen acts as an adhesive to keep bones, cartilage, skin, and blood vessels together [R]. This binding action facilitates the growth and health of our cells [R].

Sources of Pure Collagen

Collagen consists of amino acids that need to be acquired from the diet. Consuming more collagen-rich foods is a good way to increase your collagen production. 

Collagen comes mainly from animal products. These foods are rich in collagen:

  • Bone broth
  • Chicken
  • Seafood
  • Eggs
  • Fish
  • Dairy products
  • Oysters
  • Gelatin

If you are vegetarian or vegan you may not be consuming a lot of these foods. You can still get

collagen from consuming foods rich in glycine, lysine, and proline. When metabolized these compounds will produce collagen in the body [R]. 

Foods rich in these amino acids include the following [R, R, R]

  • Tempeh
  • Tofu
  • Black beans
  • Kidney beans 
  • Pumpkin seeds 
  • Sunflower seeds
  • Chia seeds
  • Pistachios
  • Peanuts 
  • Spirulina
  • Cashews

Other Nutrients Help Produce Pure Collagen

There are additional nutrients that also increase the production of collagen: 

Vitamin C, when paired with glycine and proline, will produce procollagen. This compound will turn into collagen with the addition of the mineral copper [R]. This includes the following foods:

Vitamin C [R]: 

  • Citrus fruits, berries, leafy greens, currants, elderberries, and mango

Glycine [R]: 

  • Gelatin, pork, chicken, beef, fish, ostrich, mollusks, lobster, beluga, veal, crab, seaweed, and quail

Proline [R]: 

  • Beef, pork, chicken, gelatin, soy protein, cheese, milk, and egg

Copper [R]: 

  • Mollusks, beef, veal, lamb, goose liver, oysters, seaweed, spiraling, Crimini mushrooms, lobster, and cappers

Eating foods rich in these nutrients will help to increase collagen production in the body. 

What is Hydrolyzed Collagen Powder

Pure collagen is found in cowhide and bones. These hard fibrous proteins are difficult for humans to digest [R]. To make it easy on the stomach collagen is hydrolyzed.

Hydrolyzed means that hydrolysis occurs. Hydrolysis is just a fancy way of saying water is added to the collagen. The chemical reaction that occurs when heated water is added to collagen will break the structure down into smaller more digestible pieces [R].

Once hydrolyzed the collagen will appear as a clear, odor and tasteless, powder [R]. Hydrolysis enables amino acids to be readily available for the body to absorb [R].

This new compound contains amino acids and is often referred to as collagen hydrolysate or collagen peptides [R].

Difference between Pure Collagen and Gelatin

Gelatin is collagen that has been hydrolyzed with boiling water [R]. This causes it to become a liquid and semi-liquid form similar to the texture of jelly [R].

Unlike gelatin, peptides are put through an additional process that breaks down the collagen into very tiny particles. This prevents them from forming a gel and will become soluble in both hot and cold water [R].  

Pure Collagen Health Benefits

Collagen is essential to maintain the normal structure and strength of connective tissue, such as bones, skin, cartilage, and blood vessels [R].

Collagen has been claimed to provide numerous health benefits. Research into this compound show it is important for the following: 

  • Bone health [R]
  • Joint health [R]
  • Heart health [R]
  • Muscle health [R]
  • Skin and nail health [R]
  • Gut health [R]

Health Benefits of Pure Collagen Supplements

Research suggests that collagen is a functional food and can provide a high-quality protein in ranges of 2.5 to 15 grams daily. This level of collagen has been shown to help with skin and nails, along with improvements in joint, muscle, and bone health [R]. 

Increase muscle mass

When combined with weight training collagen helped improve strength and muscle mass. A study of 53 elderly men who took 15 grams of collagen daily gained significantly more muscle more when compared with a placebo [R].

Nail and Skin Health

The production of collagen starts to taper off as we age This can lead to lines and wrinkles as early as 30 years of age [R, R, R]

Improvements in skin elasticity were seen in women when compared with a placebo. These effects lasted up to four weeks following the treatment [R]. 

Collagen is often an ingredient often added to topical face treatments. Women who given facial treatments with collagen twice daily for three months found significant improvements in lines and wrinkles within minutes of initial application continuing into the third month [R].

Nails that are brittle, rough, ragged, and peeling are a sign of protein deficiency [R]. Supplementation of 2.5 grams of collagen peptides over a 24 week period showed to have positive effects on nail health. Nails broke less often (42% less in the frequency of broken nails), increased 12 percent in growth, and global clinical improvement in brittle nails was shown. The majority of participants (80%) were completely satisfied with the results of the treatment [R].

Pure Collagen Health Benefits Where Evidence Is Lacking 

Some health claims for collagen have little or no scientific evidence to support them are actually true. 

Pure Collagen for Gut Health

To be effective foods and supplements need to be absorbed by the small intestine and delivered to the bloodstream. Often they are dissolved by stomach acids before they reach the intestinal tract. This is a critique of pure collagen peptides.

Consumption of 4.5 grams of collagen hydrolysate daily for 4 weeks changed the levels of hydroxyproline peptides in the bloodstream. This research indicated that the daily ingestion of collagen hydrolysate for a long period can affect peptide blood levels and provide beneficial effects over the long term [R]. Animal studies also found higher levels of these peptides in the blood after ingestion [R]. This illustrates how collagen peptides can increase amino acid levels which are needed for a healthy gut. 

Aside from increased peptide blood markers, there is no scientific evidence to support improvements in other gut-related issues like intestinal permeability or leaky gut. 

Pure Collagen for Weight Loss

Pure collagen has been claimed to promote weight loss and increase metabolism. 

There is no direct link between collagen and weight loss. Instead, the consumption of protein in the diet helps to improve satiety leading to fewer calories and improved weight outcomes.

A higher protein diet improves satiety and decreases the hunger hormone ghrelin. Those who are full longer will eat less and tend to lose weight [R].

Ten obese patients given gelatin (a collagen derivative) were found to have higher levels of the satiety hormone leptin [R]. 

Another study of 24 healthy adults tested the satiety effects of various protein supplements. The group who consumed breakfast with gelatin was 40 percent more satisfied than those breakfasts which did not contain collagen. Subjects that were given gelatin consumed fewer calories at lunch [R].

Collagen was shown to improve fullness and reduced food intake [R]. 

What to Look for in Pure Collagen Supplements

When picking a collagen supplement you want to make sure it comes from a grass-fed cowhide without any artificial flavors, colors, or sweeteners. 

Collagen hydrolysate or collagen peptides will be a clear and odorless powder that will mix well with both hot and cold liquids. 

The collagen powder should contain a variety of peptides. These include types I, II, III, V, and X. The incorporation of these collagen types may improve connective tissue for strong, blood vessels, skin, muscles, tendons, joints, and bones [R, R, R, R, R, R]

How to Use Pure Collagen Powder

Collagen can be used in many different ways. The clear, tasteless powder gives you the ability to mix it with any food or drink you want. 

It easily mixes with both cold and hot water. Add it to your favorite beverage, blend it in a smoothie or add it to a soup. 

Be sure to follow the serving size directions.

Pure Collagen Side Effects

The consumption of pure collagen has been generally recognized as safe not posing any major issues but some individuals have been found to have mild side effects including the following [R]: 

  • Diarrhea 
  • Rashes
  • Bloating
  • Heartburn
  • Aftertaste

More research needs to be done to find a clearer picture of the effects of collagen consumption.

Pure Collagen Contraindications

Those with an allergy or sensitivity to beef, chicken, fish, shellfish, or eggs should avoid collagen supplements with these ingredients.

Collagen intake has been shown to possibly increase oxidative stress within the body. This can be problematic for those with inflammatory conditions [R].

There is not enough research on the use of collagen use among pregnant and breastfeeding women. These populations should talk to their doctor before using collagen supplements.

Supplements are not regulated by the FDA and this goes for collagen products as well. Anyone with a health condition and/or is on medications should check with their healthcare provider before starting a collagen supplement.


Pure collagen can be helpful for a diet that is lacking in protein. It provides an abundance of amino acids that are needed to maintain many body functions. Taking collagen supplements may have some health benefits but you want to make sure you are getting a pure quality product. If you have any health or medical conditions be sure to talk to your healthcare professional before starting a supplement regimen.

69 Sources

Lodish, H. (1970, January 1). Collagen: The Fibrous Proteins of the Matrix. Retrieved from https://www.ncbi.nlm.nih.gov/books/NBK21582.

“Collagens - an Overview | ScienceDirect Topics.” n.d. Accessed March 2, 2020. https://www.sciencedirect.com/topics/neuroscience/collagens.

“What Does Collagen Mean?” n.d. https://www.definitions.net/definition/collagen.

“The Collagen Connection.” 2013. Nutrition Review. April 19, 2013. https://nutritionreview.org/2013/04/collagen-connection.

Di Lullo, Gloria A., Shawn M. Sweeney, Jarmo Korkko, Leena Ala-Kokko, and James D. San Antonio. 2002. “Mapping the Ligand-Binding Sites and Disease-Associated Mutations on the Most Abundant Protein in the Human, Type I Collagen.” The Journal of Biological Chemistry 277 (6): 4223–31. https://www.jbc.org/content/277/6/4223

Mwale, Fackson, Guoying Yao, Jean A. Ouellet, Alain Petit, and John Antoniou. 2010. “Effect of Parathyroid Hormone on Type X and Type II Collagen Expression in Mesenchymal Stem Cells from Osteoarthritic Patients.” Tissue Engineering. Part A 16 (11): 3449–55. https://www.ncbi.nlm.nih.gov/pubmed/20569194/.

Paul, Cristiana, Suzane Leser, and Steffen Oesser. 2019. “Significant Amounts of Functional Collagen Peptides Can Be Incorporated in the Diet While Maintaining Indispensable Amino Acid Balance.” Nutrients 11 (5). https://doi.org/10.3390/nu11051079.

Li, Peng, and Guoyao Wu. 2018. “Roles of Dietary Glycine, Proline, and Hydroxyproline in Collagen Synthesis and Animal Growth.” Amino Acids 50 (1): 29–38. https://www.ncbi.nlm.nih.gov/pubmed/28929384.

“Proline - an Overview | ScienceDirect Topics.” n.d. Accessed March 2, 2020. https://www.sciencedirect.com/topics/nursing-and-health-professions/proline.

Barbul, Adrian. 2008. “Proline Precursors to Sustain Mammalian Collagen Synthesis.” The Journal of Nutrition 138 (10): 2021S – 2024S. https://www.ncbi.nlm.nih.gov/pubmed/18806118

McCarty, Mark F., James H. O’Keefe, and James J. DiNicolantonio. 2018. “Dietary Glycine Is Rate-Limiting for Glutathione Synthesis and May Have Broad Potential for Health Protection.” The Ochsner Journal 18 (1): 81–87. https://www.ncbi.nlm.nih.gov/pubmed/29559876

McCarty, Mark F., James H. O’Keefe, and James J. DiNicolantonio. 2018. “Dietary Glycine Is Rate-Limiting for Glutathione Synthesis and May Have Broad Potential for Health Protection.” The Ochsner Journal 18 (1): 81–87. https://lpi.oregonstate.edu/mic/health-disease/skin-health/peptides

Porfírio, Elisângela, and Gustavo Bernardes Fanaro. 2016. “Collagen Supplementation as a Complementary Therapy for the Prevention and Treatment of Osteoporosis and Osteoarthritis: A Systematic Review” 19 (1): 153–64. http://www.scielo.br/pdf/rbgg/v19n1/1809-9823-rbgg-19-01-00153.pdf.

Balu, Darrick T., and Joseph T. Coyle. 2015. “The NMDA Receptor ‘Glycine Modulatory Site’ in Schizophrenia: D-Serine, Glycine, and beyond.” Current Opinion in Pharmacology 20 (February): 109–15. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4805108.

Chilibeck, Philip D., Mojtaba Kaviani, Darren G. Candow, and Gordon A. Zello. 2017. “Effect of Creatine Supplementation during Resistance Training on Lean Tissue Mass and Muscular Strength in Older Adults: A Meta-Analysis.” Open Access Journal of Sports Medicine 8 (November): 213–26.https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5679696

Lanhers, Charlotte, Bruno Pereira, Geraldine Naughton, Marion Trousselard, François-Xavier Lesage, and Frédéric Dutheil. 2017. “Creatine Supplementation and Upper Limb Strength Performance: A Systematic Review and Meta-Analysis.” Sports Medicine 47 (1): 163–73. https://www.ncbi.nlm.nih.gov/pubmed/27328852.

Liguori, Ilaria, Gennaro Russo, Francesco Curcio, Giulia Bulli, Luisa Aran, David Della-Morte, Gaetano Gargiulo, et al. 2018. “Oxidative Stress, Aging, and Diseases.” Clinical Interventions in Aging 13 (April): 757–72. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5927356

Kim, Hyeyoung. 2011. “Glutamine as an Immunonutrient.” Yonsei Medical Journal 52 (6): 892–97. https://www.ncbi.nlm.nih.gov/pubmed/22028151

Rao, Radhakrishna, and Geetha Samak. 2012. “Role of Glutamine in Protection of Intestinal Epithelial Tight Junctions.” Journal of Epithelial Biology & Pharmacology 5 (Suppl 1-M7): 47–54. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4369670

Wang, Lei, Timothy J. Maher, and Richard J. Wurtman. 2007. “Oral L-Glutamine Increases GABA Levels in Striatal Tissue and Extracellular Fluid.” FASEB Journal: Official Publication of the Federation of American Societies for Experimental Biology 21 (4): 1227–32. https://www.ncbi.nlm.nih.gov/pubmed/17218538.

Jing H., Cheng Y., Li S., and Zhang G. 2000. “[Effects of glutamate and glutamine on learning and memory of rats].” Wei sheng yan jiu = Journal of hygiene research 29 (1): 40–42. https://www.ncbi.nlm.nih.gov/pubmed/12725041

“Glutamine Importance for Human Health; Recent Findings and Advances | ICAAS, International Council on Amino Acid Science.” n.d. Accessed March 2, 2020. https://www.icaas-org.com/glutamine-importance-human-health-recent-findings-and-advances.

Wu, G. 2013. “21 - Arginine and Immune Function.” In Diet, Immunity and Inflammation, edited by Philip C. Calder and Parveen Yaqoob, 523–43. Woodhead Publishing. https://www.sciencedirect.com/science/article/pii/B9780857090379500217.

Wu, G. 2013. “21 - Arginine and Immune Function.” In Diet, Immunity and Inflammation, edited by Philip C. Calder and Parveen Yaqoob, 523–43. Woodhead Publishing. https://onlinelibrary.wiley.com/doi/full/10.1111/andr.12293.

PubChem. n.d. “Leucine.” https://pubchem.ncbi.nlm.nih.gov/compound/Leucine.

Hall, J. C., K. Heel, and R. McCauley. 1996. “Glutamine.” The British Journal of Surgery 83 (3): 305–12. https://pubchem.ncbi.nlm.nih.gov/compound/5961#section=Mechanism-of-Action.

Loveren and Hans Verhagen, Carlo Agostoni Jean‐louis Bresson Susan Fairweather‐tait Albert Flynn Ines Golly Hannu Korhonen Pagona Lagiou Martinus Løvik Rosangela Marchelli Ambroise Martin Bevan Moseley Monika Neuhäuser‐berthold Hildegard Przyrembel Seppo Salminen Yolanda Sanz Sean (J J. ). Strain Stephan Strobel Inge Tetens Daniel Tomé Hendrik van. 2011. “Scientific Opinion on the Substantiation of Health Claims Related to L‐glutamine and Growth or Maintenance of Muscle Mass.” https://efsa.onlinelibrary.wiley.com/doi/abs/10.2903/j.efsa.2011.2225.

PubChem. n.d. “Lysine.” https://pubchem.ncbi.nlm.nih.gov/compound/Lysine.

PubChem. n.d. “5-Hydroxylysine.” https://pubchem.ncbi.nlm.nih.gov/compound/3032849

“Hydroxylysine - an Overview | ScienceDirect Topics.” n.d. Accessed March 2, 2020. https://www.sciencedirect.com/topics/neuroscience/hydroxylysine.

Shaw, Gregory, Ann Lee-Barthel, Megan Lr Ross, Bing Wang, and Keith Baar. 2017. “Vitamin C-Enriched Gelatin Supplementation before Intermittent Activity Augments Collagen Synthesis.” The American Journal of Clinical Nutrition 105 (1): 136–43. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5183725.

Kriengsinyos, Wantanee, Mahroukh Rafii, Linda J. Wykes, Ronald O. Ball, and Paul B. Pencharz. 2002. “Long-Term Effects of Histidine Depletion on Whole-Body Protein Metabolism in Healthy Adults.” The Journal of Nutrition 132 (11): 3340–48. https://academic.oup.com/jn/article/132/11/3340/4687349.

Rui, Liangyou. 2014. “Energy Metabolism in the Liver.” Comprehensive Physiology 4 (1): 177–97. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4050641

Zhang, Shihai, Xiangfang Zeng, Man Ren, Xiangbing Mao, and Shiyan Qiao. 2017. “Novel Metabolic and Physiological Functions of Branched Chain Amino Acids: A Review.” Journal of Animal Science and Biotechnology 8 (January): 10. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5260006.

Lau, Lit-Fui, and Richard L. Huganir. 1999. Role of Tyrosine Phosphorylation in the Nervous System. Lippincott-Raven. https://www.ncbi.nlm.nih.gov/books/NBK28147.

“Valine - an Overview | ScienceDirect Topics.” n.d. https://www.sciencedirect.com/topics/neuroscience/valine.

Fernstrom, John D. 2005. “Branched-Chain Amino Acids and Brain Function.” The Journal of Nutrition 135 (6 Suppl): 1539S – 46S. https://academic.oup.com/jn/article/135/6/1539S/4663842.

Bonnans, Caroline, Jonathan Chou, and Zena Werb. 2014. “Remodelling the Extracellular Matrix in Development and Disease.” Nature Reviews. Molecular Cell Biology 15 (12): 786–801. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4316204

Paz-Lugo, Patricia de, José Antonio Lupiáñez, and Enrique Meléndez-Hevia. 2018. “High Glycine Concentration Increases Collagen Synthesis by Articular Chondrocytes in Vitro: Acute Glycine Deficiency Could Be an Important Cause of Osteoarthritis.” Amino Acids 50 (10): 1357–65. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6153947

“Foods Highest in Lysine, and Lowest in Arginine in Legumes and Legume Products.” n.d. https://nutritiondata.self.com/foods-016083000000089000000-4w.html