Sericin
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| Sericin 1 | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| Organism | |||||||
| Symbol | ser1 | ||||||
UniProt | P07856 | ||||||
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| Sericin 2 | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| Organism | |||||||
| Symbol | ser2 | ||||||
UniProt | D2WL77 | ||||||
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| Sericin 3 | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| Organism | |||||||
| Symbol | ser3 | ||||||
UniProt | A8CEQ1 | ||||||
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Sericin is a protein created by Bombyx mori (silkworms) in the production of silk.[1] Silk is a fibre produced by the silkworm in production of its cocoon. It consists mainly of two proteins, fibroin and sericin. Silk consists of 70–80% fibroin and 20–30% sericin; fibroin being the structural center of the silk, and sericin being the gum coating the fibres and allowing them to stick to each other.[2]
Structure
Sericin is composed of 18 different amino acids, of which 32% is serine. The secondary structure is usually a random coil, but it can also be easily converted into a β-sheet conformation, via repeated moisture absorption and mechanical stretching. The serine hydrogen bonds give its glue-like quality. The genes encoding sericin proteins have been sequenced. Its C-terminal part contains many serine-rich repeats.[3][4][5]
Using
Applications
Sericin has also been used in
See also
References
- ^ "Sericin". Cytokines and Cells Online Pathfinder Encyclopedia. January 2008. Retrieved 27 April 2012.
- ^ a b Padamwar MN, Pawar AP (April 2004). "Silk sericin and its applications: A review" (PDF). Journal of Scientific & Industrial Research. 63 (4): 323–329.
- PMID 9219370.
- PMID 17916509.
- PMID 19995605.
- PMID 27032876.