P5985
Protease from Bacillus sp.
liquid, ≥16 U/g
Synonym(s):
Everlase 16.0 L
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About This Item
Recommended Products
biological source
Bacillus sp.
Quality Level
form
liquid
specific activity
≥16 U/g
mol wt
20--30 kDa
storage temp.
2-8°C
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General description
Proteases are ubiquitously found in nature and microbes are the desired source for these enzymes. They are classified into four classes namely aspartic, serine, cysteine and metalloproteases.
Application
Protease from Bacillus sp. has been used to determine its proteolytic activity by spectrophotometric method.
Biochem/physiol Actions
Protease catabolizes proteins by hydrolysis of peptide bonds. Proteases are inactivated by serine active-site inhibitors, such as phenylmethylsulfonyl fluoride (PMSF) and diisopropylfluorophosphate. Proteases, secreted from Bacillus sp., typically have molecular weights ranging from 20,000 to 30,000. They are typically stabilized by Ca2+ and have high isoelectric points. It is highly soluble in detergents at a wide range of pH and temperatures. Protease improves healing process by efficiently removing necrotic materials from wounds. It is extensively used in laundry detergents to remove protein based stains from clothing. In addition, protease is also used in food, pharmaceutical, leather and silk industries. It is a key constituent in biopharmaceutical products including contact-lens enzyme cleaners and enzymatic deriders. Proteases also aid in various physiological processes such as protein turnover, digestion, blood coagulation, fertilization and cell differentiation. It also facilitates growth, cell signaling, the immune response, and apoptosis.
Legal Information
A product of Novozyme Corp.
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Aquatic Chronic 3 - Eye Dam. 1 - Resp. Sens. 1
Storage Class Code
10 - Combustible liquids
WGK
WGK 2
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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Isolation, production and characterization of protease from Bacillus sp. isolated from soil sample
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Laure El Chamy et al.
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In drosophila, molecular determinants from fungi and Gram-positive bacteria are detected by circulating pattern-recognition receptors. Published findings suggest that such pattern-recognition receptors activate as-yet-unidentified serine-protease cascades that culminate in the cleavage of Spätzle, the endogenous Toll receptor ligand, and trigger
Nicolas Buchon et al.
Proceedings of the National Academy of Sciences of the United States of America, 106(30), 12442-12447 (2009-07-11)
The Drosophila Toll receptor does not interact directly with microbial determinants, but is instead activated by a cleaved form of the cytokine-like molecule Spätzle. During the immune response, Spätzle is processed by complex cascades of serine proteases, which are activated
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