P1512
Thermolysin from Geobacillus stearothermophilus
Type X, lyophilized powder, 30-350 units/mg protein (E1%/280)
Synonym(s):
Protease from Geobacillus stearothermophilus, Thermophilic-bacterial protease
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20 MG
CN¥1,370.70
CN¥1,370.70
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20 MG
CN¥1,370.70
About This Item
CN¥1,370.70
Please contact Customer Service for Availability
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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
1 of 4
This Item | T2011 | T2327 | 650357 |
|---|---|---|---|
| biological source chicken egg white | biological source chicken egg white | biological source Glycine max (soybean) | biological source - |
| Quality Level 200 | Quality Level 300 | Quality Level 200 | Quality Level 300 |
| form powder | form powder | form lyophilized powder | form lyophilized solid |
| storage temp. 2-8°C | storage temp. 2-8°C | storage temp. 2-8°C | storage temp. −20°C |
| solubility water: soluble 10 g/L | solubility water: soluble 10 g/L | solubility - | solubility 67 mM potassium phosphate buffer, pH 7.6: 5 mg/mL |
| mol wt 14 kDa | mol wt 14 kDa | mol wt - | mol wt - |
General description
Thermolysin is a protease that has specificity different from other proteases available for sequence investigations. [1]
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. [2] It has also been used in a study to investigate the effects of sodium chloride on thermal stability and catalytic activity. [3]
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. [4]
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.
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Regulatory Information
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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
The use of thermolysin in amino acid sequence determination.
R P Ambler et al.
The Biochemical journal, 108(5), 893-895 (1968-08-01)
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
Yongjin Park et al.
Scientific reports, 12(1), 10935-10935 (2022-06-30)
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
Friedrich Hans Kleiner et al.
Journal of cell science, 134(9) (2021-09-23)
Cytochrome c6 is a redox carrier in the thylakoid lumen of cyanobacteria and some eukaryotic algae. Although the isofunctional plastocyanin is present in land plants and the green alga Chlamydomonas reinhardtii, these organisms also possess a cytochrome c6-like protein designated
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