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Ingredients/Compound/Sericin

Sericin.

Strength pending.The research strength is not set yet.

A silk protein about a third serine. Taken by mouth it's digested like any protein and contributes amino acids. On skin it dries into a water-holding film.

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SericinIngredientMD
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Compound

What Sericin is, and what it does.

Does it work
Suits someone building a skin-focused routine or curious about a serine-rich protein. Anyone reacting to silk, dust mite or other insect proteins should avoid it.
How much to take
No dose figure is on record for oral use, so we won't invent one. Topical products carry their own concentration. Start with what the product in front of you states.
Time to feel it
On skin, the film forms immediately and you notice it after one application. Oral timing hasn't been mapped in people.
The first dose
Topically, skin feels smoother and holds water within minutes. Taken by mouth, day one adds serine and glycine to your amino acid pool.
With regular use
Weeks of topical use is where the hydration work sits. For weeks of oral use, nobody has measured the outcome in people yet.
How well tolerated
Well tolerated on skin for most people. It is a known occupational allergen around silk processing, so anyone sensitive to insect or dust mite proteins should avoid it.
How it feels
On skin, a light slippery film that dries soft rather than tacky. Swallowed, it behaves like any dietary protein, so the effect sits in your amino acid intake.
The overlooked benefit
Serine feeds glycine and cysteine production, so a protein that is a third serine contributes to pathways well past simple tissue building.

The proof, claim by claim.

These words describe the research, not the molecule's worth. Research strength is how much work stands behind one claim, and it is never a product score.

  • Skin hydration with topical useRandomised trial
  • Serine-rich amino acid contribution from oral proteinNarrative review
  • Metal chelation and slowed oxidation in laboratory systemsIn vitro study
  • Glucose metabolism markers in animal modelsAnimal study
  • Occupational allergen in silk processingNarrative review
PubMedCochraneClinicalTrials.govNIH ODSSUPP.AILabs test. IngredientMD verifies.PubMedCochraneClinicalTrials.govNIH ODSSUPP.AILabs test. IngredientMD verifies.
Pairs well with7 on file

Why these belong in the same formula. Each row says what the basis is, from settled biochemistry through to a trial that measured the pair.

Sericin + GlycineSericin is an unusually serine-rich protein, and serine and glycine interconvert directly through serine hydroxymethyltransferase.

Roughly a third of sericin's amino acid residues are serine, with aspartic acid and glycine making up much of the rest. Digested sericin therefore delivers serine, which SHMT converts to glycine while transferring a one-carbon unit to folate. Glycine supplementation feeds the same interconversion from the other side. This is amino acid biochemistry, not a demonstrated clinical pairing.

Sericin + L-serineSericin's dominant residue is serine, so it functions as a dietary serine source once hydrolysed.

Oral sericin is digested to peptides and free amino acids like any other protein. Because of its composition, the amino acid it supplies most is serine. Free L-serine supplies the same residue without the peptide step. Which of the two is preferable depends on whether the peptide fraction is wanted, and that has not been settled.

Sericin + Chromium picolinateA rat study reported that sericin consumption changed chromium picolinate handling.

The work was done in rats and measured chromium exposure and downstream metabolic markers rather than clinical outcomes in people. Peptides can enhance trace mineral uptake by keeping the metal soluble in the intestinal lumen, which is a known mechanism for other peptide fractions. Whether this holds in humans has not been tested. Read it as mechanistic rather than clinical.

Sericin + ProbioticsA human tolerability study of sericin-derived oligopeptides reported shifts in gut microbiota composition alongside its tolerability data.

Peptide fractions that resist upper gut digestion become substrate for colonic bacteria. The human work reported shifts in microbiota composition alongside gastrointestinal tolerability data. A change in composition is a marker, not an outcome, and the direction of any benefit was not established. The pairing with a defined probiotic strain has not been tested at all.

Sericin + Hyaluronic acidBoth are hydrophilic film formers used together in topical and biomaterial work.

Sericin's hydroxyl-rich serine residues bind water and leave a flexible film on drying. Hyaluronic acid holds water in the same layer through a different polymer chemistry. Combining them is standard practice in hydrogel and topical formulation for humectancy and film integrity. This is a formulation property and says nothing about oral use.

Sericin + Collagen peptidesBoth are hydrolysed protein fractions used together in the same product categories.

Collagen peptides supply glycine, proline and hydroxyproline. Sericin supplies serine, aspartate and glycine. The amino acid profiles complement rather than duplicate each other. In topical and hydrogel work they also co-form films. The combination is a formulation choice, and no trial has tested the pair for any endpoint.

Sericin + GlutathioneSericin is described as having metal-chelating and radical-scavenging activity in laboratory systems.

The reported antioxidant behaviour of sericin comes from cell-free and cell culture systems, where its hydroxyl-rich residues chelate transition metals and slow metal-catalysed oxidation. Glutathione works enzymatically inside cells, which is a different compartment and a different mechanism. Any additive effect is theoretical at this point. Do not read laboratory antioxidant activity as an effect in people.

Who should be cautious

Nothing specific on file for Sericin. Match the label to the daily amount above, and tell your doctor what you take.

Not medical advice. Show the label to your pharmacist.

What Sericin actually does.

Established

Sericin is the sticky protein that glues silk fibers together in the cocoon. the process that softens silk washes this protein away, which is why it used to just be a waste byproduct rather than something sold on its own.

Established

About a third of sericin's building blocks are the amino acid serine, along with aspartic acid, glycine and threonine. that composition is heavy on hydroxyl groups, which is why it dissolves in water and holds onto moisture so strongly.

Established

If you eat it, sericin gets digested just like any other protein, broken into amino acids and small peptides, it doesn't reach your bloodstream in one piece. so the part of oral use that actually makes biochemical sense is its contribution of amino acids.

Established

When it dries, sericin forms a continuous water-loving film. that's why it's used in skin products and gels, it's a physical property, not a biological effect on the body.

Animal-sourced, 6 steps on record

Where Sericin comes from.

Sericin is the sticky protein that glues a silkworm cocoon together. Making silk soft means washing it off, so for most of history it went down the drain. It is about a third serine, an amino acid, and it holds water well, which is why it turns up in both drinks and skin products.

Made from an animal material. Species and tissue are the things worth knowing, and both belong on a label.

Starts as
Bombyx mori cocoons

Silkworm cocoons, including yellow cocoon varieties which carry a different pigment and flavonoid profile from white. Sericin is roughly a quarter to a third of the cocoon by weight.

Extracted by
Degumming

Cocoons are boiled in water, dilute alkali, soap solution or with proteases. This dissolves the sericin coating and releases the fibroin filaments. Historically the sericin-bearing water was discarded as effluent.

Converted by
Hydrolysis

The recovered protein is hydrolysed enzymatically or chemically to reduce molecular weight. Enzymatic routes give a narrower and more reproducible peptide distribution than acid or alkaline routes.

Purified by
Filtration and desalting

Membrane filtration removes salts, residual detergent and fibroin fragments, and can fractionate by molecular weight.

Standardised to
Molecular weight fractionation

Material is characterised by molecular weight distribution and protein content. This is the specification that actually distinguishes one sericin from another.

Ends up as
Spray-dried powder or aqueous solution

Supplied as a spray-dried powder for oral and dry formats, or as a preserved aqueous solution for topical use.

Cocoon colour and whether the degumming used enzymes, alkali or soap are rarely stated on a label, and both change the finished material.

The forms it comes in.

Hydrolysed sericinAcid, alkaline or enzymatic hydrolysis breaks the native protein into shorter peptides with lower average molecular weight.Fits Beverages and oral formats where solubility and low viscosity matter.Trade-off Hydrolysis conditions set the peptide profile, so two hydrolysates with the same name can behave differently. Harsh acid or alkaline routes also degrade some residues.
SDO, defined oligopeptide fractionEnzymatically produced and fractionated to a narrow molecular weight band, which is the material used in the reported human work.Fits Studies and products where a defined and reproducible fraction is required.Trade-off More expensive to produce, and the fractionation spec has to be disclosed for the name to mean anything.
Native sericinExtracted with minimal chain scission, retaining the long-chain structure and its gelling behaviour.Fits Hydrogels, films and biomaterial scaffolds where mechanical properties matter.Trade-off Poor cold-water solubility and it gels on cooling, which makes it awkward in beverages.Formulation aid
Sericin, aqueous cosmetic gradeAqueous solution preserved for topical use, usually mid-range molecular weight for film formation without stickiness.Fits Leave-on skin and hair products relying on humectancy and film forming.Trade-off Requires a preservative system, and topical performance data does not transfer to oral use in any direction.Formulation aid
Sericin hydrogelChemically or physically crosslinked network with tuned swelling and degradation behaviour.Fits Biomaterial and controlled-release research applications.Trade-off Crosslinker chemistry has to be documented, and this is a materials format rather than a supplement one.Formulation aid
What the strongest studies found

The essence, in one line each.

  1. Sericin-derived oligopeptides from yellow silk cocoons were tolerated in the tested dose range and were accompanied by shifts in gut microbiota composition.Open-label trial. Oo-Puthinan S et al., 2026 (Foods). PMID 42450525
  2. Adding sericin to freezing and thawing media changed measured sperm quality parameters after cryopreservation.In vitro study. Aghaz F et al., 2020 (The Aging Male). PMID 30453816
  3. Sericin added to a semen freezing extender improved post-thaw quality measures and fertility rate in roosters.Animal study. Ratchamak R et al., 2023 (Animal Bioscience). PMID 37170513
  4. Sericin in the freezing extender improved post-thaw sperm quality measures in goats, with changes in glutamine metabolism reported alongside.Animal study. Yu Y et al., 2025 (Animals). PMID 41096425
  5. Sericin supplementation of freezing media altered heat shock protein 70 expression and redox measures in post-thaw semen.Animal study. Reddy VS et al., 2018 (Cryobiology). PMID 30098997
  6. Sericin added before and during in vitro maturation reduced the damage seen when oocytes were exposed to hydrogen peroxide.In vitro study. Yindeetrakul S et al., 2026 (Veterinary Medicine International). PMID 42180161
  7. Silk-derived sericin changed how heterotypic cell spheroids formed and how they responded to metformin in culture.In vitro study. Calvo-Chica LE et al., 2026 (Biomaterials Advances). PMID 42335554

These are the studies our verdict leans on, chosen from the 7 we read for Sericin. The full linked list is below.

Primary evidence

The studies, linked.

8 sources behind our Sericin verdict: peer-reviewed studies and registered clinical trials. Every one links straight to PubMed, the journal, or ClinicalTrials.gov. Read them yourself.

  1. ClinicalTrials.gov
  2. ClinicalTrials.gov
  3. ClinicalTrials.gov
  4. ClinicalTrials.gov
  5. ClinicalTrials.gov
  6. ClinicalTrials.gov
  7. ClinicalTrials.gov
  8. ClinicalTrials.gov

Evidence surfaced via Semantic Scholar (Allen Institute for AI) and ClinicalTrials.gov. Ranked by study type and citation weight, not cherry-picked.

FDA Disclaimer: These statements have not been evaluated by the Food and Drug Administration. This information is for educational purposes only and is not intended to diagnose, treat, cure, or prevent any disease. Consult your healthcare provider before starting any supplement regimen.