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What Happens to Collagen You Drink?

Studies

What happens in the body when you drink collagen? We explain what research shows, together with the reasons some say it is pointless.

Why Some Say It Is Pointless

Key point: collagen you drink is absorbed after being broken down

  • Digestion○ Into amino acids and small peptides
  • Blood○ Peptides such as Pro-Hyp are found

Collagen you drink does not become the body’s collagen as is. On the other hand, some of it enters the blood as small peptides without being fully broken down.

*This summarizes research findings; it does not claim that collagen does or does not work.

You may hear that collagen supplements are “pointless” or “have no effect.” Here are the common reasons, side by side with what research shows.

Common claimWhat research shows
It just becomes amino acidsIt is digested into peptides and amino acids, but small peptides such as Pro-Hyp have been found in the blood
It is a low-quality proteinIt lacks the essential amino acid tryptophan and is classed as an incomplete protein by PDCAAS

Source:[1]、[2]、[3]

Collagen Is Broken Down by Digestion

Collagen is one of the proteins that make up the body. Like other proteins, collagen that is eaten or drunk is digested in the stomach and intestines into peptides (short chains of amino acids) and amino acids before it is absorbed. So collagen you drink does not become the body’s collagen in its original large form.

From drinking collagen to the blood

Simplified diagram

Collagen (peptides) you drinkDigested in stomach and gutAmino acidsSingle unitsSmall peptidese.g. Pro-Hyp (2–3 units)Absorbed into the blood

The main reason people call it pointless is this breakdown. However, as the next section shows, research has found that some of it enters the blood as small peptides without being fully broken down.

Source:[1]、[2]

Collagen Peptides Found in the Blood

Collagen is rich in an amino acid called hydroxyproline (Hyp). Using it as a marker, researchers can see what form collagen takes in the blood after drinking it. Studies by Japanese universities and companies report the following.

Study (subjects)Findings
Japan, Kyoto Prefectural University et al. (2005)
Healthy people; 9.4–23 g gelatin hydrolysate from pig skin, chicken feet and cartilage
Almost no peptide-form Hyp before; it rose after ingestion, peaked at 1–2 h (20–60 nmol/mL plasma) and fell to half the peak at 4 h. The main peptide was Pro-Hyp
Japan (2007)
5 healthy men; fish scale, fish skin, pig skin
About 30% of the Hyp detected in blood was in peptide form; the amount and type of peptides differed by source
Japan, company study (2010)
People given gelatin hydrolysate
Nine Hyp-containing peptides were measured; the most abundant was Pro-Hyp (peak about 61 nmol/mL)
Japan, Kyoto Prefectural University et al. (2011)
5 people; collagen hydrolysate
Pro-Hyp was found in all 5 and Hyp-Gly in 4; their ratio varied by person

Peptide-form Hyp in blood, before and after

Approximate, with the peak as 100 (from the 2005 abstract)

≈0Peak≈HalfBefore1–2 h4 h

Form of Hyp found in blood (2007 study)

All Hyp detected = 100%

≈30%≈70%■ Peptide form■ Free Hyp (amino acid)

Cell experiments on the peptides found

The 2011 study reported that Hyp-Gly was less easily broken down by blood enzymes than Pro-Hyp, and in experiments with mouse fibroblasts (cells that make collagen), it increased cell growth more than Pro-Hyp. These are cell experiments; whether the same happens in the human body must be tested separately.

All these studies were small and measured blood after ingestion. Peptides entering the blood and changes occurring in the body are separate questions. Researchers from a food company took part in the 2007 and 2010 studies.

Source:[4]、[2]、[5]、[6]、[7]

Collagen as a Protein

One way to compare protein quality is PDCAAS (Protein Digestibility-Corrected Amino Acid Score). By this method, collagen is classed as an incomplete protein because it lacks tryptophan, one of the essential amino acids the body cannot make.

On the other hand, a 2019 study calculated that, based on a standard American diet, up to 36% of daily protein could be replaced with collagen peptides while still meeting essential amino acid requirements. The amounts used in past studies (2.5–15 g per day) fall within that range. The authors include company researchers and a researcher who provides research services to a maker of supplements containing collagen peptides.

In short, collagen alone cannot cover protein needs, but added to an ordinary diet it does not upset the balance of protein.

Source:[3]

FAQ

Is drinking collagen pointless?
That cannot be said definitively. Ingested collagen is digested, but some enters the blood as small peptides.

Does collagen you drink become the body’s collagen as is?
No. It is first broken down into amino acids and small peptides, then absorbed.

How long do the peptides stay in the blood?
A 2005 study reported that they peaked 1–2 hours after ingestion and fell to half the peak at 4 hours.

Do we get collagen from ordinary food?
Japanese women are estimated to take in about 2 g of collagen a day from their diet.

How much is used in studies?
Past studies have used about 2.5–15 g per day.

Source:[1]、[2]、[3]

Sources

  1. [1]Kimira Y., Mano H. (Josai University), Journal for the Integrated Study of Dietary Habits 25(1), 2014
    https://www.jstage.jst.go.jp/article/jisdh/25/1/25_005/_article/-char/ja/
  2. [2]Iwai K, et al. J Agric Food Chem 2005;53:6531-6536
    https://pubmed.ncbi.nlm.nih.gov/16076145/
  3. [3]Paul C, et al. Nutrients 2019;11:1079
    https://pmc.ncbi.nlm.nih.gov/articles/PMC6566836/
  4. [4]Okuyama K. (Osaka University), Journal of the Crystallographic Society of Japan 54(5), 2012
    https://www.jstage.jst.go.jp/article/jcrsj/54/5/54_263/_article/-char/ja
  5. [5]Ohara H, et al. J Agric Food Chem 2007;55:1532-1535
    https://pubmed.ncbi.nlm.nih.gov/17253720/
  6. [6]Ichikawa S, et al. Int J Food Sci Nutr 2010;61:52-60
    https://pubmed.ncbi.nlm.nih.gov/19961355/
  7. [7]Shigemura Y, et al. Food Chem 2011;129:1019-1024
    https://pubmed.ncbi.nlm.nih.gov/25212331/

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