P5985
Protease from Bacillus sp.
liquid, ≥16 U/g
Sinônimo(s):
Everlase 16.0 L
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About This Item
Produtos recomendados
fonte biológica
Bacillus sp.
Formulário
liquid
atividade específica
≥16 U/g
peso molecular
20--30 kDa
temperatura de armazenamento
2-8°C
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Descrição geral
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.
Aplicação
Protease from Bacillus sp. has been used to determine its proteolytic activity by spectrophotometric method.
Ações bioquímicas/fisiológicas
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.
Informações legais
A product of Novozyme Corp.
Palavra indicadora
Danger
Frases de perigo
Declarações de precaução
Classificações de perigo
Aquatic Chronic 3 - Eye Dam. 1 - Resp. Sens. 1
Código de classe de armazenamento
10 - Combustible liquids
Classe de risco de água (WGK)
WGK 2
Equipamento de proteção individual
dust mask type N95 (US), Eyeshields, Faceshields, Gloves
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Irreversible inhibitors of serine, cysteine, and threonine proteases
Powers JC, et al.
Chemical Reviews, 102(12), 4639-4750 (2002)
Isolation, production and characterization of protease from Bacillus sp. isolated from soil sample
Josephine FS, et al.
Journal of Microbiology, 2(1), 163-168 (2012)
Laure El Chamy et al.
Nature immunology, 9(10), 1165-1170 (2008-08-30)
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
M Du et al.
Journal of animal science, 85(4), 919-927 (2006-12-21)
Mammalian target of rapamycin (mTOR) signaling is one of the main signaling pathways controlling protein synthesis. Leucine treatment upregulates mTOR signaling, which enhances protein synthesis; however, the mechanisms are not well understood. Herein, treatment of C2C12 myoblast cells with leucine
Effect of UV light on microbial proteases: From enzyme inactivation to antioxidant mitigation.
Lante A, et al.
Innovative Food Science & Emerging Technologies, 17, 130-134 (2013)
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