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P5985

Sigma-Aldrich

Protease from Bacillus sp.

liquid, ≥16 U/g

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Synonym(s):
Everlase 16.0 L
EC Number:
MDL number:
NACRES:
NA.54

biological source

Bacillus sp.

form

liquid

specific activity

≥16 U/g

mol wt

20--30 kDa

storage temp.

2-8°C

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This Item
P3111P5860P1236
form

liquid

form

liquid

form

liquid

form

liquid

specific activity

≥16 U/g

specific activity

≥16 U/g

specific activity

≥8 U/g

specific activity

≥0.8 U/g

mol wt

20--30 kDa

mol wt

20-30 kDa

mol wt

20--30 kDa

mol wt

-

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

2-8°C

Quality Level

200

Quality Level

200

Quality Level

200

Quality Level

200

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.

Pictograms

CorrosionHealth hazard

Signal Word

Danger

Hazard 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

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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)
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)
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
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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