ChemicalBook--->CAS DataBase List--->9014-01-1

9014-01-1

9014-01-1 Structure

9014-01-1 Structure
IdentificationBack Directory
[Name]

EC 3.4.21.14
[CAS]

9014-01-1
[Synonyms]

sp266
nagarse
AlcalMe
Superase
maxatase
bioprase
alk-enzyme
colistinase
YN-NL Amano
Spezyme FAN
Savinase 4T
Savinase 6T
Savinase TM
Sumizyme CP
Savinase 8.0
e.c.3.4.4.16
SUBTILISIN A
EC 3.4.21.14
Savinase 8.0L
Savinase 8.0T
Savinase 4.0T
Subtilisin KL
Subtilisin DFE
Tricozyme ML 3
PROTEASELIQUID
PROTEASEPOWDER
subtilisinbpn’
subtilisinnovo
thermoasepc-10
Alcalase? 2.4L
Protease type Ⅷ
Savinase L16 EX
Subtilopeptidase
subtilopeptidaseb
subtilopeptidasec
PROTEASE ALKALINE
bacillopeptidasea
bacillopeptidaseb
protease type xxxi
Savinase 32.0 L-EX
Savinase Ultra 16L
Alkaline proteinase
subtilisincarlsburg
subtilopeptidasebpn’
Subtilisin Carslberg
Serine alkaline protease
bacillussubtiliscarlsberg
Protease from Bacillus sp.
Validase TSP Concentrate II
Novozymes protease, alkaline
protease type viii bacterial
SubtilisinExBacillusSubtilis
ALCALASEFROMBACILLUSLICHENIFORMIS
Protease from Subtilisin carlsberg
Subtilisin A, Bacillus lichenformis
protease from bacillus licheniformis
protease for total dietary fiber assay
subtilisin from bacillus licheniformis
proteinase from bacillus licheniformis
SubtilisinexBacillussubtilis=Subtilisin
Subtilisin,from Bacillus luchenformis
Bacillussubtilisenzymefermentationproduct
Proteinase Bacillus subtilis var. biotecus A
Novozymes protease, alkaline and thermostable
PROTEINASE FROM BACILLUS LICHENIFORMIS, ~8 U/MG
SUBTILISIN FROM BACILLUS LICHENIFORMIS, ~6 U/MG
proteinase from bacillus subtilis var. biotecus a
protease bacterial (subtilisin*carlsberg) aseptic
Protease Bacillus globigii (Bacillus licheniformis)
SUBTILISIN FROM BACILLUS LICHENIFORMIS, ~12 UNITS/MG
PROTEASE BACTERIAL (SUBTILISIN*CARLSBERG ) ASEPTICAL
proteinase from bacillus subtilis var. biotecus A ~20 U/mg
Subtilisin Carlsberg from Bacillus subtilis var. biotecus A
Proteinase from Bacillus licheniformis, Subtilisin(R) A, Subtilisin(R) Carslberg
Protease from Bacillus licheniformis,Proteinase from Bacillus licheniformis, Subtilisin A, Subtilisin Carslberg
Protease from Bacillus licheniformis,Alcalase 2.4L, Proteinase from Bacillus licheniformis, Subtilisin A, Subtilisin Carslberg
Protease from Streptomyces griseus, Subtilo peptidase A, Subtilisin(R) Carlsberg from Bacillus subtilis var. biotecus A
Alkaline Protease, Protease from Bacillus licheniformis, Proteinase from Bacillus licheniformis, Subtilisin(R) Carlsberg, Subtilo peptidase A
Proteinase, bacterial,Alkaline Protease, Protease from Bacillus licheniformis, Proteinase from Bacillus licheniformis, Subtilisin Carlsberg, Subtilo peptidase A
[EINECS(EC#)]

232-752-2
[Molecular Formula]

NULL
[MDL Number]

MFCD00165548
Chemical PropertiesBack Directory
[Appearance]

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

1.3
[vapor pressure ]

0Pa at 25℃
[storage temp. ]

2-8°C
[form ]

powder
[color ]

white
[biological source]

Bacillus sp.
[Water Solubility ]

100g/L at 25℃
[Specific Activity]

7-15units/mg solid
[Stability:]

store cold
[Major Application]

food and beverages
[Cosmetics Ingredients Functions]

SKIN CONDITIONING
KERATOLYTIC
[LogP]

-3.1 at 25℃
[CAS DataBase Reference]

9014-01-1
[EPA Substance Registry System]

Subtilisin (9014-01-1)
Safety DataBack Directory
[Symbol(GHS) ]

Corrosion (GHS05)Exclamation Mark (GHS07)Health Hazard (GHS08)Environment (GHS09)
GHS05,GHS07,GHS08,GHS09
[Signal word ]

Danger
[Hazard statements ]

H302-H315-H318-H334-H335-H410
[Precautionary statements ]

P261-P273-P280-P301+P312-P302+P352-P305+P351+P338
[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
[OEL]

STEL: 0.00006 mg/m3 [60-minute]
[RIDADR ]

3082
[WGK Germany ]

2
[RTECS ]

UK9540000
[F ]

3-10
[TSCA ]

TSCA listed
[REACH Registrations]

Active
[HS Code ]

35079090
[Storage Class]

11 - Combustible Solids
[Hazard Classifications]

Acute Tox. 4 Oral
Aquatic Acute 1
Aquatic Chronic 2
Eye Dam. 1
Resp. Sens. 1
Skin Irrit. 2
STOT SE 3
[Hazardous Substances Data]

9014-01-1(Hazardous Substances Data)
[Toxicity]

LD50 orl-rat: 3700 mg/kg FCTXAV 7,581,69
Hazard InformationBack Directory
[Potential Exposure]

These commercial proteolytic enzymes are used in laundry detergent formulations
[First aid]

If this chemical gets into the eyes, remove any contact lenses at once and irrigate immediately for at least 15 minutes, occasionally lifting upper and lower lids. Seek medical attention immediately. If this chemical contacts the skin, remove contaminated clothing and wash immediately with soap and water. Seek medical attention immediately. If this chemical has been inhaled, remove from exposure, begin rescue breathing (using universal precautions, including resuscitation mask) if breathing has stopped and CPR if heart action has stopped. Transfer promptly to a medical facility. When this chemical has been swallowed, get medical attention. Give large quantities of water and induce vomiting. Do not make an unconscious person vomit.
[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.
[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).
[Biosynthesis]

Biosynthetically, subtilin is produced from a ribosomally derived pre-pro-peptide by a series of post-translational modifications. [1]
[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.
[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.]
[Toxics Screening Level]

The initial threshold screening level (ITSL) for subtilisins is 0.0006 μg/m 3 (1-hour averaging time).
[References]

[1]Burrage, Sarah Anne. Biomimetic synthesis of subtilin. Diss. University of Southampton, 1998
Questions And AnswerBack Directory
[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.
	EC 3.4.21.14
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