Which Collagen? Bovine vs. Marine vs. Chicken

Posted by Stars + Honey Team on

Key Points:

    1. Bovine collagen, when compared to other collagen sources, is the most like human collagen and therefore most easily recognized by the human body.
    2. While bovine collagen prior to being hydrolyzed has a larger molecular size than marine collagen this difference can equalize once bovine collagen is broken down into peptides.
    3. Bovine collagen is more efficient to produce and is more easily traceable than marine collagen.
    4. People more often report side effects with marine and chicken collagen than they do when consuming bovine collagen.

Bovine Collagen 

Bovine collagen that is extracted from the bones, cartilage, and skin (hide) of cows is the most abundant and favorable form, as the structure of bovine collagen particles is biologically similar to that of human collagen [1, 2]. This means the body easily recognizes and absorbs bovine collagen after it is consumed. There are very few reports of digestive discomfort following the use of bovine collagen [1-3]. Bovine collagen is also an excellent source of key amino acids such as glycine, proline, and hydroxyproline—vital building blocks for natural collagen production [1].

When pure, native collagen is extracted from bovine sources, the particles are larger than marine or chicken collagen particles, but careful processing procedures gently reduce the size of the particles. More specifically, bovine collagen particles are broken down into peptides (small chains of amino acids)—also called hydrolyzed collagen or collagen hydrolysate—that are easily digested and absorbed by the intestines [2]. This is why many people who take bovine collagen have reported  regularly experiencing marked health benefits without unpleasant reactions. The abundance of bovine sources and resourceful processing procedures also makes the use of bovine collagen cost-effective—a factor that offers reasonable pricing for consumers.

Another important point is that regular supplementation with bovine collagen is more efficient than other forms (e.g., chicken, marine) at heightening collagen type I, II, and III production in the human body [5]. These three forms of collagen are abundant throughout the entire body. Therefore, people who consume a potent source of bovine collagen daily often report positive experienced benefits in the skin, hair, nails,  bones, joints and muscles [2, 5, 6].

Marine Collagen

Marine collagen is typically extracted from the bones, skin, fins, and scales of a wide variety of marine species. However, marine sources mostly consist of type I collagen, the form that is primarily produced by the body to support hair, nail, and skin health [1]. Small amounts of type II collagen have also been detected in some marine sources, but it does not contain collagen type III.

The collagen particles that are extracted from marine sources are smaller than bovine and chicken collagen and are easily absorbed, but they do not offer the same concentration or types of amino acids or the forms of collagens that bovine and chicken sources provide [7]. This limitation is demonstrated through research which shows that marine collagen supports healthy skin, but is less efficient at targeting other areas of health (e.g., joint, bone) [1, 7].

One of the problems with marine collagen is that the source is not always clearly listed on the label. This is because ‘marine’ is a collective term that refers to any aquatic species, including shellfish, shark, and jellyfish. In addition, marine collagen may produce a 'fishy' odor and processing is often more expensive and less consistent than processing procedures for bovine or chicken collagen.

Furthermore, marine sources of collagen are not as easy for the immune system to recognize because the structure does not closely resemble that of human collagen [1, 7]. Some people have also reported digestive discomfort following marine collagen consumption along with an unpleasant taste in the mouth. Individuals with fish or shellfish allergies also must be careful when consuming marine collagen, as the source is not always clearly listed.

The use of marine collagen for supplements and cosmetics is still fairly new. Due to issues such as a ‘fishy’ taste and odor, possible stomach upset, potential allergic reactions, and expensive production costs, marine collagen is not currently a popular option.

Chicken Collagen

Collagen that is extracted from chicken feet is another source of this structural protein [1, 3]. Chicken feet are typically discarded as waste, but with increasing interest in alternative sources of collagen, poultry producers suggest that chicken by-products such as feet, bones, and skin offer low manufacturing costs for chicken collagen [8].

Chicken collagen offers similar benefits as bovine collagen but it is not widely used in cosmetics and dietary supplements. Some people who consume chicken collagen experience mild to moderate side effects (e.g., stomach upset, constipation, skin reactions, headaches) – which is not typically the case with bovine collagen from our examination of the research reports and general consumer reviews.

The immune system in the human body appears to detect chicken collagen as a foreign invader. In some cases, the immune system may gradually begin to recognize chicken collagen particles and improve the body’s response to it. However, this does not always occur, possibly resulting in unexpected side effects or new symptoms for some people.

Most people respond well to bovine collagen because the particles are biologically similar to collagen produced by the human body [1, 2, 4]. This is one of the main reasons that bovine collagen is the primary type that is found in various products, including cosmetics and dietary supplements.


Bovine collagen is most commonly found in supplements due to its structural similarity to human collagen, the ease of absorption and digestion, and its good safety profile. This form of collagen is also more efficient at boosting natural collagen production throughout the body than marine or chicken collagen, because bovine collagen provides ideal amounts of types I and III as well as sufficient amounts of type II.

Marine collagen is limited to mostly collagen type I and small amounts of collagen type II. The structure of chicken collagen is similar to bovine collagen, but has an increased risk of unwanted immune responses.


  1. Rodriguez MIA, Barroso LGR, Sanchez ML. Collagen: A review on its sources and potential cosmetic applications. J Cosmet Dermatol. 2018;17(1):20-26.
  2. Asserin J, Lati E, Shioya T, Prawitt J. The effect of oral collagen peptide supplementation on skin moisture and the dermal collagen network: evidence from an ex vivo model and randomized, placebo-controlled clinical trials. J Cosmet Dermatol. 2015;14(4):291-301.
  3. Wang H. A review of the effects of collagen treatment in clinical studies. Polymers (Basel). 2021;13(22): 3868.
  4. de Moraes LO, Lodi FR, Gomes TS, et al. Immunohistochemical expression of types I and III collagen antibodies in the temporomandibular joint disc of human foetuses. Eur J Histochem. 2011;55(3):e24.
  5. Leon-Lopez A, Morales-Penzloza A, Martinez-Juarez VM, et al. Hydrolyzed-collagen—Sources and applications. Molecules. 2019;24(22):4031-4047.
  6. Jendricke P, Centner C, Zdzieblik D, et al. Specific collagen peptides in combination with resistance training improve body composition and regional muscle strength in premenopausal women: A randomized controlled trial. Nutrients. 2019;11(4):892-904.
  7. Gomes-Guillen MC, Gimenez B, Lopez-Caballero ME, et al. Functional and bioactive properties of collagen and gelatin from alternative sources: A review. Food Hydrocolloids. 2011;25(8):1813-1827.
  8. Santana JC, Gardim RB, Almeida PF, e.t al Valorization of chicken feet by-product of the poultry industry: High qualities of gelatin and biofilm from extraction of collagen. Polymers. 2020;12:529.
  9. Crowley DC, Lau FC, Sharma P, et al. Safety and efficacy of undenatured type II collagen in the treatment of osteoarthritis of the knee: A clinical trial. Int J Med Sci. 2009;6(6):312-321.



← Older Post Newer Post →