|recombinant||expressed in E. coli BL21|
|mol wt||mol wt ~39 kDa|
|pH-range||5.5 - 12.5 (optimum activity is seen at pH 12.5)|
This enzyme contains a C-terminus 6-Histidine tag.
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.
Keratin. Keratinases have also been used for the degradation of prion and prion-like proteins.
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.
Keratinase is a non-specific serine protease that cleaves non-terminal peptide bonds.
Keratinase is activated by 0.10% SDS, 1.0% CTAB, and EDTA. Keratinase is partially inhibited by Tween®20, DMSO, isopropanol, methanol, and ethanol.
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Bacterial keratinases: useful enzymes for bioprocessing agroindustrial wastes and beyond. Brandelli, A. Food Bioprocess Tech. 1, 105-116, (2008)
Screening for a new Streptomyces strain capable of efficient keratin degradation. Chao, Y. P. et al. J. Environ. Sci. Health 19, 1125-28, (2007)
In vitro degradation of porcine skin epidermis by a fungal keratinase of Doratomyces microsporus. Enzyme Microb. Technol. 36, 450-460, (2005)
Similarities and specificities of fungal keartinolytic proteases: comparison of keratinases of Paecilomyces marquandii and Doratomyces microspores to some known proteases. Gradisar, H. et al. Appl. Environ. Microbiol. 71, 3420-3426, (2005)
Expression of the Bacillus licheniformis PWD-1 keratinase gene in B. Subtilis. Lin, X. et al. J. Ind. Microbiol. 19, 134-138, (1997)
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