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Specific activity:
≥16 U/g
Biological source:
Bacillus sp.
Servicio técnico
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Permítanos ayudarlebiological source
Bacillus sp.
Quality Segment
form
liquid
specific activity
≥16 U/g
mol wt
20--30 kDa
storage temp.
2-8°C
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.
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Danger
hcodes
Hazard Classifications
Aquatic Chronic 3 - Eye Dam. 1 - Resp. Sens. 1
Clase de almacenamiento
10 - Combustible liquids
wgk
WGK 2
ppe
dust mask type N95 (US), Eyeshields, Faceshields, Gloves
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