K4519
Keratinase
lyophilized powder
Synonim(y):
Keratinase from Bacillus licheniformis, KerA, Keratinolytic protease
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About This Item
Polecane produkty
rekombinowane
expressed in E. coli BL21
Poziom jakości
Postać
lyophilized powder
aktywność właściwa
300-1000 units/mg protein
masa cząsteczkowa
~39 kDa
zakres pH
5.5-12.5(optimum activity is seen at pH 12.5)
pI
8.73
temp. przechowywania
−20°C
Opis ogólny
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.
Zastosowanie
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.
Działania biochem./fizjol.
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.
Właściwości fizyczne
Keratinase is activated by 0.10% SDS, 1.0% CTAB, and EDTA. Keratinase is partially inhibited by Tween®20, DMSO, isopropanol, methanol, and ethanol.
Definicja jednostki
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.
Uwaga dotycząca przygotowania
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.
Substraty
Keratin. Keratinases have also been used for the degradation of prion and prion-like proteins.
Inne uwagi
This enzyme contains a C-terminus 6-Histidine tag.
Informacje prawne
TWEEN is a registered trademark of Croda International PLC
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Hasło ostrzegawcze
Warning
Zwroty wskazujące rodzaj zagrożenia
Zwroty wskazujące środki ostrożności
Klasyfikacja zagrożeń
Acute Tox. 4 Oral - Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3
Organy docelowe
Respiratory system
Kod klasy składowania
11 - Combustible Solids
Klasa zagrożenia wodnego (WGK)
WGK 3
Certyfikaty analizy (CoA)
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Klienci oglądali również te produkty
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
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
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
Keratinolytic activity from the broth of a feather-degrading thermophillic Streptomyces thermoviolaceus strain SD8.
Chitte RR, Nalawade VK, Dey S.
Letters in Applied Microbiology, 28, 131-136 (1999)
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