For research use only. Not for therapeutic Use.
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
Thermolysin (100 μg in 1 mL, 64°C for 4 h, in isolated starch granules) digestion results in the selective removal of a group of low-molecular-mass proteins ranging between 10 and 27 kD[2].
Thermolysin can be used for the hydrolysis of bovine liver sarcoplasmic proteins[3].
Thermolysin (50 mg/kg, p.o., once) lowers systolic blood pressure in SHR rats[4].
Thermolysin is not acutely toxic with an oral LD50 of more than 18000 mg/kg in rats and more than 24000 mg/kg in mice (Acute toxicity studies)[5].
| Catalog Number | I042552 |
| CAS Number | 9073-78-3 |
| Purity | ≥95% |
| Reference | [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. |
