Thermolysin, Bacillus thermoproteolyticus rokko

Thermolysin, Bacillus thermoproteolyticus rokko (EC 3.4.24.27) (TML) is a thermostable neutral metalloproteinase enzyme secreted by the Gram-positive bacteria Bacillus thermoproteolyticus. Thermolysin catalyzes the hydrolysis of peptide bonds containing hydrophobic residues[1].Optimal pH: 8.0. Considerably stable from pH 5 to 9.5. Optimal temperature : 70 °C

Product Specifications

CAS Number

[9073-78-3]

Product Name Alternative

EC 3.4.24.27; TML

UNSPSC

12352204

Hazard Statement

H334

Target

Endogenous Metabolite

Type

Enzyme

Related Pathways

Metabolic Enzyme/Protease

Applications

COVID-19-immunoregulation

Field of Research

Infection

Assay Protocol

https://www.medchemexpress.com/thermolysin-bacillus-thermoproteolyticus-rokko.html

Purity

Solubility

H2O : ≥ 1 mg/mL

Smiles

[Thermolysin]

Precautions

H334

References & Citations

[1]Bertusvan den Burg, et al. Chapter 111 - Thermolysin and Related Bacillus Metallopeptidases. |[2]Mu-Forster C, et al. Surface localization of zein storage proteins in starch granules from maize endosperm. Proteolytic removal by thermolysin and in vitro cross-linking of granule-associated polypeptides. Plant Physiol. 1998 Apr;116 (4) :1563-71. |[3]Di Bernardini R, et al. Isolation, purification and characterization of antioxidant peptidic fractions from a bovine liver sarcoplasmic protein thermolysin hydrolyzate. Peptides. 2011 Feb;32 (2) :388-400. |[4]Fujita H, et al: a prodrug-type ACE-inhibitory peptide derived from fish protein. Immunopharmacology. 1999 Oct 15;44 (1-2) :123-7. |[5]Ke Q, et al. Safety evaluation of a thermolysin enzyme produced from Geobacillus stearothermophilus. Food Chem Toxicol. 2013 Sep;59:541-8.