P1512
Thermolysin from Geobacillus stearothermophilus
Type X, lyophilized powder, 30-350 units/mg protein (E1%/280)
Synonyme(s) :
Protease from Geobacillus stearothermophilus, Thermophilic-bacterial protease
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About This Item
Produits recommandés
Source biologique
Geobacillus stearothermophilus
Niveau de qualité
Type
Type X
Forme
lyophilized powder
Activité spécifique
30-350 units/mg protein (E1%/280)
Poids mol.
34.6 kDa by amino acid sequence
Produit purifié par
crystallization
Conditions d'expédition
wet ice
Température de stockage
−20°C
Description générale
Thermolysin is a protease that has specificity different from other proteases available for sequence investigations.
Application
A thermostable (thermophilic) extracellular metalloendopeptidase containing four calcium ions. Cofactors are zinc and calcium. Hydrolyzes protein bonds on the N-terminal side of hydrophobic amino acid residues. The pH optimum is 8.0 and the optimal temperature for activity is 70 °C. Considerably stable from pH 5 to 9.5. Thermolysin has a low cleavage specificity, therefore, it produces a number of short fragments that are suitable for sequencing. Preferential cleavage: X-cleavage-Y-Z where X=any amino acid; Y=Leu, Phe, Ile, Val, Met, Ala and Z is any amino acid other than Pro. Cleavage N-terminal to Leu is preferred over cleavage of N-terminal to Phe which is preferred over the others. Often used to do limited proteolysis for peptide mapping and studies of protein structure and conformational changes.
Thermolysin has been shown to have a prosequeence that acts as an intramolecular chaperone in vivo. It has also been used in a study to investigate the effects of sodium chloride on thermal stability and catalytic activity.
Thermolysin is also commonly used for the commercial synthesis of N-(benzyloxycarbonyl)-L-aspartyl-L-phenylalanine methyl ester, the precursor for the artificial sweetener aspartame.
Qualité
Contains many extraneous enzymes.
Définition de l'unité
One unit will hydrolyze casein to produce color equivalent to 1.0 μmole (181 μg) of tyrosine per min at pH 7.5 at 37 °C (color by Folin-Ciocalteu reagent).
Forme physique
lyophilized powder containing calcium and sodium acetate buffer salts
Notes préparatoires
The pH optimum is 8.0 and the optimal temperature for activity is 70 °C. Considerably stable from pH 5 to 9.5. Thermolysin has a low cleavage specificity, therefore, it produces a number of short fragments that are suitable for sequencing. Preferential cleavage: X-cleavage-Y-Z where X=any amino acid; Y=Leu, Phe, Ile, Val, Met, Ala and Z is any amino acid other than Pro. Cleavage N-terminal to Leu is preferred over cleavage of N-terminal to Phe which is preferred over the others.
Mention d'avertissement
Danger
Mentions de danger
Conseils de prudence
Classification des risques
Resp. Sens. 1
Code de la classe de stockage
11 - Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 3
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Équipement de protection individuelle
dust mask type N95 (US), Eyeshields, Faceshields, Gloves
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Les clients ont également consulté
K Inouye et al.
Biochimica et biophysica acta, 1388(1), 209-214 (1998-10-17)
Thermolysin, a thermophilic metalloproteinase, is markedly activated in the presence of high concentrations (1-5 M) of neutral salts. The activity increases in an exponential fashion with increasing salt concentration, and is enhanced 13-15 times with 4 M NaCl at pH
The use of thermolysin in amino acid sequence determination.
R P Ambler et al.
The Biochemical journal, 108(5), 893-895 (1968-08-01)
M Miyanaga et al.
Biotechnology and bioengineering, 46(6), 631-635 (1995-06-20)
N-(benzyloxycarbonyl)-L-aspartyl-L-phenylalanine methyl ester, a precursor of the synthetic sweetener, aspartame, was synthesized from N-(benzyloxycarbonyl)-L-aspartic acid and L-phenylalanine methyl ester with an immobilized thermolysin (EC 3.4.24.4) in the mixed organic solvent system of tert-amyl alcohol and ethyl acetate. A mixed solvent
Balbir K Chaal et al.
Methods in molecular biology (Clifton, N.J.), 390, 207-217 (2007-10-24)
All the algae with chlorophyll (Chl) c (haptophytes, cryptophytes, and heterokonts such as diatoms) acquired their chloroplasts by secondary endosymbiosis, where a nonphotosynthetic eukaryote host engulfed (or was invaded by) a red alga. This resulted in chloroplasts with four bounding
Haley Marshall et al.
Acta crystallographica. Section D, Biological crystallography, 68(Pt 1), 69-81 (2011-12-24)
Both crystallization and cryoprotection are often bottlenecks for high-resolution X-ray structure determination of macromolecules. Methylamine osmolytes are known stabilizers of protein structure. One such osmolyte, trimethylamine N-oxide (TMAO), has seen occasional use as an additive to improve macromolecular crystal quality
Protocoles
To standardize a procedure for the enzymatic assay of Protease using Casein as a substrate.
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