Silk amino acid (SAA)

Last Updated: September 28 2022

SAAs are amino acids derived from the Silkworm cocoon, containing the peptide compounds Sericin-S and Sericin-L (small and large). Hydrolyzed SAAs are needed to be digested, and SAAs appear to be very nice compounds for skin, hair, and nail health when orally ingested.

Silk amino acid (SAA) is most often used for


Silk Amino Acids are a mixture of amino acids obtained from the cocoon of the Silk Worm Bombix Mori. The mixture of amino acids is very high in the amino acids serine and aspartate, and some versions are rich in tyrosine as well.

The protein can be found in a hydrolyzed (pre-digested) form known as Sericin-S, or as a undigestible form known as Sericin-L. The undigestible form appears to exert protective effects on the colon and intestinal tract, whereas the hydrolyzed form can beneficially affect systemic (post-intestinal) metabolic functions.

Sericin also appears to beneficially affect the skin, in both a protective sense (anti-oxidation, anti-UV radiation) as well as increasing moisture content. These effects may be seen with both topical application or ingestion.

It looks to be a promising compound, but no human studies on health have been conducted.

What else is Silk amino acid (SAA) known as?
Note that Silk amino acid (SAA) is also known as:
  • Sericin
  • SAA
  • SAAa
Dosage information

There is insufficient evidence to recommend an optimal dosage of silk amino acids for human supplementation, although it is known that for any purpose where silk amino acids need to be absorbed a hydrolyzed form of the supplement is required. Hydrolyzed silk amino acids are not required if the target are the intestines or colon.

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1.^Terada S, Sasaki M, Yanagihara K, Yamada HPreparation of silk protein sericin as mitogenic factor for better mammalian cell cultureJ Biosci Bioeng.(2005 Dec)
2.^Kato N, Sato S, Yamanaka A, Yamada H, Fuwa N, Nomura MSilk protein, sericin, inhibits lipid peroxidation and tyrosinase activityBiosci Biotechnol Biochem.(1998 Jan)
4.^Tsujimoto K, Takagi H, Takahashi M, Yamada H, Nakamori SCryoprotective effect of the serine-rich repetitive sequence in silk protein sericinJ Biochem.(2001 Jun)
5.^Dugo P, Donato P, Cacciola F, Germanò MP, Rapisarda A, Mondello LCharacterization of the polyphenolic fraction of Morus alba leaves extracts by HPLC coupled to a hybrid IT-TOF MS systemJ Sep Sci.(2009 Nov)
8.^Sato W, Fukumoto K, Yanagihara K, Sasaki M, Kunitomi Y, Terada SMitogenic effect of sericin on mammalian cellsBMC Proc.(2011 Nov 22)
9.^Even MS, Sandusky CB, Barnard NDSerum-free hybridoma culture: ethical, scientific and safety considerationsTrends Biotechnol.(2006 Mar)
10.^Yanagihara K, Terada S, Miki M, Sasaki M, Yamada HEffect of the silk protein sericin on the production of adenovirus-based gene-therapy vectorsBiotechnol Appl Biochem.(2006 Sep)
11.^Shin S, Yeon S, Park D, Oh J, Kang H, Kim S, Joo SS, Lim WT, Lee JY, Choi KC, Kim KY, Kim SU, Kim JC, Kim YBSilk amino acids improve physical stamina and male reproductive function of miceBiol Pharm Bull.(2010 Feb)
13.^Okazaki Y, Kakehi S, Xu Y, Tsujimoto K, Sasaki M, Ogawa H, Kato NConsumption of sericin reduces serum lipids, ameliorates glucose tolerance and elevates serum adiponectin in rats fed a high-fat dietBiosci Biotechnol Biochem.(2010)
18.^Padamwar MN, Pawar AP, Daithankar AV, Mahadik KRSilk sericin as a moisturizer: an in vivo studyJ Cosmet Dermatol.(2005 Dec)