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K4519

Sigma-Aldrich

Keratinase

lyophilized powder

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Synonym(s):
Keratinase from Bacillus licheniformis, KerA, Keratinolytic protease
Enzyme Commission number:
NACRES:
NA.54

recombinant

expressed in E. coli BL21

Quality Level

form

lyophilized powder

specific activity

300-1000 units/mg protein

mol wt

~39 kDa

pH range

5.5-12.5(optimum activity is seen at pH 12.5)

pI 

8.73

storage temp.

−20°C

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This Item
O9515P5380P8038
vibrant-m

K4519

Keratinase

vibrant-m

O9515

Prolyl oligopeptidase

vibrant-m

P8038

Proteinase, bacterial

form

lyophilized powder

form

solution

form

lyophilized powder

form

lyophilized powder

recombinant

expressed in E. coli BL21

recombinant

expressed in E. coli

recombinant

-

recombinant

-

storage temp.

−20°C

storage temp.

−70°C

storage temp.

−20°C

storage temp.

−20°C

mol wt

~39 kDa

mol wt

81.6 kDa

mol wt

27 kDa

mol wt

27 kDa

Quality Level

200

Quality Level

200

Quality Level

200

Quality Level

300

General description

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

Application

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.

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.

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.

Unit Definition

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.

Preparation Note

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.

Substrates

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

Other Notes

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

Legal Information

TWEEN is a registered trademark of Croda International PLC

pictograms

Exclamation mark

signalword

Warning

Hazard Classifications

Acute Tox. 4 Oral - Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3

target_organs

Respiratory system

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3


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Customers Also Viewed

Helena Gradisar et al.
Applied and environmental microbiology, 71(7), 3420-3426 (2005-07-08)
Based on previous screening for keratinolytic nonpathogenic fungi, Paecilomyces marquandii and Doratomyces microsporus were selected for production of potent keratinases. The enzymes were purified and their main biochemical characteristics were determined (molecular masses, optimal temperature and pH for keratinolytic activity
Bacterial Keratinases: Useful Enzymes for Bioprocessing Agroindustrial Wastes and Beyond.
Brandelli A
Food and Bioprocess Technology, 1(2), 105-116 (2008)
Ellen J Beswick et al.
The Journal of infectious diseases, 187(8), 1291-1300 (2003-04-16)
The role of glycosaminoglycans (GAGs) in the invasion of host cells by Chlamydia pneumoniae strains TW-183 and A-03 was investigated and compared with the role of invasion by C. trachomatis serovars L2 and E. The quantities of epithelial and endothelial
Beti Vidmar et al.
Food technology and biotechnology, 56(3), 312-328 (2018-12-05)
Keratin is a complex and structurally stable protein found in human and animal hard tissues, such as feathers, wool, hair, hoof and nails. Some of these, like feathers and wool, represent one of the main sources of protein-rich waste with
Cheng-gang Cai et al.
Journal of Zhejiang University. Science. B, 9(1), 60-67 (2008-01-16)
A new feather-degrading bacterium was isolated from a local feather waste site and identified as Bacillus subtilis based on morphological, physiochemical, and phylogenetic characteristics. Screening for mutants with elevated keratinolytic activity using N-methyl-N'-nitro-N-nitrosoguanidine mutagenesis resulted in a mutant strain KD-N2

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