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P1512

Sigma-Aldrich

Thermolysin from Geobacillus stearothermophilus

Type X, lyophilized powder, 30-350 units/mg protein (E1%/280)

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Synonym(s):
Protease from Geobacillus stearothermophilus, Thermophilic-bacterial protease
CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
eCl@ss:
32160410

biological source

Geobacillus stearothermophilus

Quality Level

type

Type X

form

lyophilized powder

specific activity

30-350 units/mg protein (E1%/280)

mol wt

34.6 kDa by amino acid sequence

purified by

crystallization

shipped in

wet ice

storage temp.

−20°C

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T7902P8038T9935
Proteinase, bacterial Type XXIV, 7.0-14.0 units/mg solid, lyophilized powder

P8038

Proteinase, bacterial

Trypsin from bovine pancreas essentially salt-free, lyophilized powder, ≥9,000 BAEE units/mg protein, BioReagent, suitable for cell culture

T9935

Trypsin from bovine pancreas

biological source

Geobacillus stearothermophilus

biological source

Geobacillus stearothermophilus

biological source

-

biological source

-

form

lyophilized powder

form

powder

form

lyophilized powder

form

essentially salt-free, lyophilized powder

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

shipped in

wet ice

shipped in

-

shipped in

wet ice

shipped in

-

mol wt

34.6 kDa by amino acid sequence

mol wt

34.6 kDa

mol wt

27 kDa

mol wt

23.8 kDa

General description

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.

Quality

Contains many extraneous enzymes.

Unit Definition

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).

Physical form

lyophilized powder containing calcium and sodium acetate buffer salts

Preparation Note

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.

pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

dust mask type N95 (US), Eyeshields, Faceshields, Gloves


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Customers Also Viewed

C Marie-Claire et al.
Journal of molecular biology, 285(5), 1911-1915 (1999-02-02)
The zinc metalloendopeptidase, thermolysin (EC 3.4.24.27) produced by Bacillus thermoproteolyticus serves as a model of important physiological enzymes such as neprilysin, angiotensin converting enzyme and endothelin converting enzyme. Thermolysin is synthesised as a pre-proenzyme, with an N-terminal prosequence of 204
Chiwook Park et al.
Nature methods, 2(3), 207-212 (2005-03-23)
Thermodynamic stability is fundamental to the biology of proteins. Information on protein stability is essential for studying protein structure and folding and can also be used indirectly to monitor protein-ligand or protein-protein interactions. While clearly valuable, the experimental determination of
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Viral entry is the first stage in the virus replication cycle and, for enveloped viruses, is mediated by virally encoded glycoproteins. Viral glycoproteins have different receptor affinities and triggering mechanisms. We employed vesicular stomatitis virus (VSV), a BSL-2 enveloped virus
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Long wavelengths that can deeply penetrate into human skin are required to maximize therapeutic effects. Hence, various studies on near-infrared organic light-emitting diodes (NIR OLEDs) have been conducted, and they have been applied in numerous fields. This paper presents a
The use of thermolysin in amino acid sequence determination.
R P Ambler et al.
The Biochemical journal, 108(5), 893-895 (1968-08-01)

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