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9025-41-6

9025-41-6 Structure

9025-41-6 Structure
IdentificationBack Directory
[Name]

Keratinase
[CAS]

9025-41-6
[Synonyms]

keratinase
Keratinase, Streptomyces
[EINECS(EC#)]

232-793-6
Chemical PropertiesBack Directory
[storage temp. ]

-20°C
[form ]

Cream colored powder
[Appearance]

Light Yellow Powder
[PH]

7 - 9
[Water Solubility ]

Partially miscible in water
[Specific Activity]

300-1000units/mg protein
[EPA Substance Registry System]

Keratinase, Streptomyces (9025-41-6)
Safety DataBack Directory
[TSCA ]

TSCA listed
Hazard InformationBack Directory
[Physical properties]

Keratinase is activated by 0.10% SDS, 1.0% CTAB, and EDTA. Keratinase is partially inhibited by Tween?20, DMSO, isopropanol, methanol, and ethanol.
[Uses]

Keratinase is used in the dehairing of hides and skins:In depilatory compositions for human use: Mattin, Greenstein, US 2988485 (1961 to Mearl).
[Uses]

Keratinase may be used for enzymatic treatment of elementary body (EB), GAG molecules, and cells in the study of the role glycosaminoglycans (GAGs) in the invasion of host cells by Chlamydia pneumoniae strains.
[General Description]

Keratinase is also metalloprotease present in bacteria as well as eukaryotes. Keratinase isolated from Bacilus licheniformis culture is a monomeric enzyme.
[Biochem/physiol Actions]

Keratinase is a particular class of extracellular proteolytic inducible enzyme with the capability of degrading insoluble keratin substrates. It is important for hydrolyzing hair, feather, and collagen in sewage system during waste water treatment. It is also useful in food industry, animal feed preparation etc. Insoluble feather keratin from poultry industry may be converted by enzymatic hydrolysis to glues, feedstuffs, fertilizers, films or used for the production of rare amino acids serine, cysteine and proline.
[References]

[1] X LIN. Purification and Characterization of a Keratinase from a Feather-Degrading Bacillus licheniformis Strain.[J]. ACS Applied Electronic Materials, 1992: 3271-3275. DOI:10.1128/aem.58.10.3271-3275.1992.
[2] BETI VIDMAR Ma?a V. Microbial Keratinases: Enzymes with Promising Biotechnological Applications.[J]. Food Technology and Biotechnology, 2018, 56 3: 312-328. DOI:10.17113/ftb.56.03.18.5658.
[3] ELLEN J BESWICK Morris D C Anna Travelstead. Comparative studies of glycosaminoglycan involvement in Chlamydia pneumoniae and C. trachomatis invasion of host cells.[J]. Journal of Infectious Diseases, 2003, 187 8: 1291-1300. DOI:10.1086/374056.
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