EC 3.4.21.14 Chemical Properties

Density 

1.3

vapor pressure 

0Pa at 25℃

storage temp. 

2-8°C

form 

powder

color 

white

Water Solubility 

100g/L at 25℃

Stability:

store cold

LogP

-3.1 at 25℃

CAS DataBase Reference

9014-01-1

EPA Substance Registry System

Subtilisin (9014-01-1)

Safety Information

Hazard Codes 

Xn,N

Risk Statements 

37/38-41-42-36/37/38-50-22

Safety Statements 

23-24-26-36/37/39-22-36/37-61-45-39

RIDADR 

3082

OEL

STEL: 0.00006 mg/m3 [60-minute]

WGK Germany 

2

RTECS 

UK9540000

F 

3-10

HS Code 

35079090

Hazardous Substances Data

9014-01-1(Hazardous Substances Data)

Toxicity

LD50 orl-rat: 3700 mg/kg FCTXAV 7,581,69

EC 3.4.21.14 Usage And Synthesis

Defination

Proteases (EC 3.4.21.62) belong to the class of enzymes known as hydrolases, which catalyze hydrolysis of various bonds in presence of water. Proteases are also referred to as Peptidases or Proteinases. Proteases catalyze proteolysis of peptide bonds in polypeptides, proteins and selective hydrolysis of carboxylic esters and amino esters. There are different classes of Proteases, i.e. serine, threonine, cysteine, aspartate, glutamic acid and metallo – proteases.

Chemical Properties

These are proteolytic enzymes which take the form of light-colored, free-flowing powders. A protein containing numerous amino acids

Uses

This is a proteolytic enzyme isolated from the fermentation of Bacillus licheniformis. It is a serine endoproteinase with a broad specificity towards native and denatured proteins, and is active under alkaline conditions. It is for use in Total Dietary Fiber Assays (TDF-100A).

Uses

Protease from Bacillus licheniformis has been used to digest the neurolemma in the antennal lobe of the moth; Heliothis virescens.

Uses

Protease from Bacillus sp. has been used to determine its proteolytic activity by spectrophotometric method.

General Description

Proteolytic enzymes are known to possess catalytic, non-catalytic and ancillary domains. Proteases are broadly classified as endopeptidases and exopeptidases. Functionally they are divided as aspartic, glutamic, cysteine, threonine, serine and metalloproteases.

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 typcially stabilized by Ca2+ and have high isoelectric points.

Safety Profile

Moderately toxic by ingestion. Aneye irritant. When heated to decomposition it emits toxicfumes of NOx.

Potential Exposure

These commercial proteolytic enzymes are used in laundry detergent formulations

Purification Methods

This alkaline protease is purified 211-fold by affinity chromatography using 4-(4-aminophenylazo)phenylarsonic acid complex to activated CH-Sepharose 4B. It is inhibited by 2-phenylethane boronic acid, PMSF, 3,4-dichloroisocoumarin, acetone and benzamide. [Chandraskaren & Dhar Anal Biochem 150 141 1985, Schomburg & Schomburg Springer Handbook of Enzymes 2nd Edn vol 7 p 286 2002.] Synexin (from bovine liver) M 47,000 Da. This Ca binding protein is purified by (NH4)2SO4 precipitation, then by a specific pH step elution from a chromatofocusing medium in the absence of ampholytes. The pI is 7.5. [Scott et al. Anal Biochem 149 163 1985.]

Incompatibilities

Incompatible with oxidizers (chlorates, nitrates, peroxides, permanganates, perchlorates, chlorine, bromine, fluorine, etc.); contact may cause fires or explosions. Keep away from alkaline materials, strong bases, strong acids, oxoacids, epoxides.

EC 3.4.21.14(9014-01-1)Related Product Information

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• TRIS(2,2,6,6-TETRAMETHYL-3,5-HEPTANEDIONATO)DYSPROSIUM(III)
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• 1,1,3,3-TETRAMETHYLBUTYL ISOCYANIDE
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• EC 3.4.21.14