Keratinase

Keratin. Keratinases have also been used for the degradation of prion and prion-like proteins.

Keratinase is a non-specific serine protease that cleaves non-terminal peptide bonds. This enzyme is active between 37°- 70°C. The highest activity is typically seen at 70°C.

Keratinase is activated by 0.10% SDS, 1.0% CTAB, and EDTA. Keratinase is partially inhibited by Tween^®20, DMSO, isopropanol, methanol, and ethanol.

Keratinase is also metalloprotease present in bacteria as well as eukaryotes. Keratinase isolated from Bacilus licheniformis culture is a monomeric enzyme.

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.

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.

The enzyme can be solubilized at 0.5-1.0 mg/mL in either sterile water or phosphate buffer. The best activity is seen with freshly prepared solutions. However, single-use aliquots of Keratinase solutions can be stored at -20° C.

One unit of enzyme is able to hydrolyze casein resulting in an absorbance value as the Folin-Ciocalteau reagent equivalent to 1 umole (181μg) of tyrosine per minute at pH 7.5 at 37 °C.

This enzyme contains a C-terminus 6-Histidine tag.

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