ChemicalBook--->CAS DataBase List--->9001-92-7

9001-92-7

9001-92-7 Structure

9001-92-7 Structure
IdentificationBack Directory
[Name]

PROTEASE
[CAS]

9001-92-7
[Synonyms]

QN 20
ZY 88
Tamase
Recepin
Siro NL
Vernase
PRONASE
PROLASE
NEWLASE
NAGARASE
PROTEASE
Ronozyme
Sputazyme
Umimazyme
a.s.1.398
Protizyme
PROZYME 6
ACTINASE E
Protezyn L
Protex 89L
Veron L 10
PROTEINASE
Tunicase F
Ultralizin
Ultrazym P
Rodazym ML
Sumizyme BP
Sumizyme OP
Sumizyme RP
Validase FP
EC 3.4.23.6
EC 3.4.24.4
Protex 50FP
Purafect OxP
PROTEINASE 6
PROTEINASE A
PROTEASE A-1
milezyme APL
SUBTILISIN A
EC 3.4.21.14
EC 3.4.21.62
EC 3.4.23.18
AUXILLASE(R)
Variante F49
Thermoase PS
Toyozyme NEP
Riberzym MPX
Peptidase R
SEBPro FL 100
Savinase 12TK
Unikneutral L
Sumizyme LP50
ENDOPEPTIDASE
PROTEINASE 2A
Proteinase DS
Protease 
Purafect 4000E
Purafect 3450M
Proteopol FP-t
PROTEASE HIV-1
Purafect Prime
Sumizyme ACP-G
Savinase 18.0T
Ronozyme ProAct
PROTEASE, CRUDE
Protex Gentle L
PROTEASE TYPE I
PROTEASE TYPE X
Proteinase 
Protease oryzae
ALCALASE(R) CLEA
protease m amano
from Aspergillus
SEBrite BP 16.0L
Sukazym-SukaproNE
Tasinase N-11-100
Proteinase SP 446
Neutro-Proteinase
BACTERIALPROTEASE
PROTEASE TYPE XIX
SUBTILOPEPTIDASE A
PROTEASE TYPE VIII
PROTEASE TYPE XIII
ALCALASE(R) ENZYME
PROTEASE TYPE XXIV
REC HIV-1 PROTEASE
Proteinase AS1.398
Validase Actinidin
Ronozyme ProAct CT
protease from hiv-1
Relase Ultra 16L EX
Proteinase Type XXⅢ
protease type xxvii
PROTEASE A 'AMANO2'
PRONASE(R) PROTEASE
PROTEASE TYPE XVIII
PROTEASE TYPE XXIII
Flavourzyme, 20u/mg
SUBTILISIN CARLSBERG
MICROBIALPROTEINASES
Purafect Prime 4000L
Fungal Acid Protease
PROTEINASE, BACTERIAL
Proteinase Type XXIII
Native Bovine Protease
from Bacillus subtilis
PROTEASE, NUCLEASE-FREE
Enzyme Pepsin Food grade
Bacillus polymyxa neutral
PROTEASE, FROM ASPERGILUS
Protease from Aspergillus
Peptidase Rhizopus oryzae
ASPERGILLOPEPTIDASE MOLSIN
Proteasefrombovinepancreas
ENDOTHIACARBOXYLPROTEINASE
protease from rhizopus sp.
ASPERGILLUS ACID PROTEINASE
HIV-1 PROTEASE, RECOMBINANT
Nonspecific neutral protease
PROTEASEFROMASPERGILLUSNIGER
Native Rhizopus sp. Protease
Neutral Protease for pet food
Neutral Protease AF GMP Grade
PROTEASEFROMASPERGILLUSORYZAE
proteinase A from bakers yeast
PEPTIDASE FROM RHIZOPUS ORYZAE
protease from aspergillus sojae
protease from bacillus polymyxa
PROTEINASE, BACTERIAL, ~10 U/MG
bacillussubtilisneutralprotease
PROTEASE (STREPTOMYCES GRISEUS)
PROTEASE (SUBTILISIN CARLSBERG)
SUBTILISIN CARLSBERG, BACTERIAL
HIV Protease (Wild Type Q7K)
proteinase from bacillus subtilis
Native Aspergillus oryzae Protease
Proteasefromstreptomycescaespitosus
EndoproteinaseAsp-N,Sequencinggrade
ALCALASE(R), BACILLUS LICHENIFORMIS
protease type I from bovine pancreas
Subtilisin(R) Carlsberg, bacterial
Native Aspergillus melleus Proteinase
Native Bacillus licheniformis Protease
protease from clostridium histolyticum
protease type xv from bacillus polymyxa
Native Bacillus licheniformis Proteinase
BACILLUSSUBTILIS-DERIVEDDETERGENTPROTEASE
Native Bacillus amyloliquefaciens Protease
protease type xxiii from aspergillus*oryzae
Protease, from Bacillus subtilis, >=3 units/mg
Neutral Protease for Beer Brewing (Food Grade)
protease type xix fungal from*aspergillus sojae
protease hiv-1 recombinant expressed in E. coli
proteinase a from baker's yeast (s. cerevisiae)
protease attached to agarose from*staphylococcus
protease type xviii fungal from*rhizopus species
Neutral Protease froM Bacillus polyMyxa(Purified)
endoproteinase asp-N from pseudomonas*fragi (muta
Neutral Protease NB from Clostridium histolyticum
Native Bacillus polymyxa Neutral Protease (Dispase)
PROTEASE ATTACHED TO AGAROSE FROM*STAPHYLOCOCCUS AUR
PROTEASE ATTACHED TO AGAROSE FROM*STAPHY LOCOCCUS AU
alpha-N-Benzoyl-DL-arginine-p-nitroanilide hydrolase
Endoproteinase Asp-N, ExcisionGrade, Pseudomonas fragi
Native Flavobacterium menigosepticum Endoproteinase AspN
endoproteinase asp-n from pseudomonas fragi mutant strain
Neutral Protease NB GMP Grade from Clostridium histolyticum
Native Pseudomonas fragi mutant strain Endoproteinase Asp-N
Neutral Protease from Bacillus polymyxa(Partially Purified)
Protease from Streptomyces griseus, Subtilo peptidase A
PROTEASE FROM BACILLUS LICHENIFORMIS, CROSS-LINKED ENZYME AGGREGATE
ProteasefromstreptomycescaespitosussubstantiallyfreeofDnaseiiandRnase.
Neutral Protease NB High Active Grade froM ClostridiuM histolyticuM purified
Protease-Agarose 4% cross-linked beaded agarose from Staphylococcus aureus V8
[EINECS(EC#)]

232-990-7
[Molecular Formula]

NULL
[MDL Number]

MFCD00132092
Chemical PropertiesBack Directory
[storage temp. ]

2-8°C
[solubility ]

H2O: 5-20 mg/mL
[form ]

powder
[color ]

white
[biological source]

Streptomyces griseus
[Water Solubility ]

water: soluble 10-20g/L
[Specific Activity]

≥5units/mg solid
[Cosmetics Ingredients Functions]

SKIN CONDITIONING
[EPA Substance Registry System]

Proteinase (9001-92-7)
Safety DataBack Directory
[Symbol(GHS) ]

Exclamation Mark (GHS07)Health Hazard (GHS08)
GHS07,GHS08
[Signal word ]

Danger
[Hazard statements ]

H315-H319-H334-H335
[Precautionary statements ]

P302+P352-P305+P351+P338
[Hazard Codes ]

Xn
[Risk Statements ]

37/38-41-42-36/37/38
[Safety Statements ]

23-24-26-36/37/39-36/37-22-45
[WGK Germany ]

3
[RTECS ]

UK9595000
[F ]

3-10
[TSCA ]

TSCA listed
[HS Code ]

35079010
[Storage Class]

11 - Combustible Solids
[Hazard Classifications]

Resp. Sens. 1
[Toxicity]

LD50 ipr-mus: 45 mg/kg CYLPDN 4,214,83
Raw materials And Preparation ProductsBack Directory
[Raw materials]

LACQUER THINNER-->streptomyces avermifilis
Hazard InformationBack Directory
[Chemical Properties]

nearly white to light brown amorphous powder or liquid. Soluble in water, the aqueous solution generally appears pale yellow. It is virtually insoluble in ethanol, chloroform, and ether. Its primary function is to hydrolyze proteins into low-molecular-weight peptones, urea, polypeptides, and amino acids. Naturally occurring in animals, plants, and microorganisms, its industrial applications are primarily those produced by molds. The protein produced by Aspergillus oryzae has an optimum temperature of 45-50°C at a pH of 6.0. Proteins produced by Aspergillus niger (Asp. niger 3350) and Bacillus cereus (B. cereus), also known as acid-resistant proteinase, have an optimum pH of 2.5 and an optimum temperature of 45°C. Copper or manganese ions at a concentration of 2×10-3 mol strongly activate it, while silver and mercury ions have an inhibitory effect.
[Uses]

Protease from Rhizopus spp. Has been used in a study to assess the amino acid sequences near the amino termini using automated Edman degradation. It has also been used in a study to investigate inactivation of the enzyme by reaction with diazoacetyl-DL-norleucine methyl ester in the presence of cupric acetate.
[General Description]

Proteases belong to the group of hydrolases and exist as acid, neutral, and alkaline proteases.
[Biochem/physiol Actions]

Proteases catabolize proteins by hydrolysis of peptide bonds. They have many applications such as in detergents, bioremediation processes, pharmaceutical industry, and food industries. Proteases are associated with nitrogen mineralization in the soil. They also serve as a supplement in swine and poultry diets.
[Safety Profile]

A poison by intraperitoneal route.When heated to decomposition it emits acrid smoke andirritating vapors.
[Toxics Screening Level]

The initial threshold screening level (ITSL) for Proteinase is 0.0006 μg/m3 (1-hour averaging time).
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