Thermolysin


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Related to Thermolysin: trypsin

Ther`mo`ly´sin


n.1.(Biochem.) a proteolytic enzyme obtained from the bacterium Bacillus thermoproteolyticus, which hydrolyses the N-terminal amide bonds of hydrophobic amino acid residues in proteins. It is used in studies of protein structure. It has a molecular weight of about 37,500 and contains zinc and calcium in its active configuration.
Webster's Revised Unabridged Dictionary, published 1913 by G. & C. Merriam Co.
References in periodicals archive ?
For instance, recently, thermolysin enzyme intended for use in dairy products to improve taste, protein solubility and digestibility of dairy products has been recognized as GRAS.
Among the digests of the water-insoluble protein fraction prepared from muscle, a thermolysin digest demonstrated the highest activity among those that were tested.
They contain enzymes from different origins, such as collagenases from higher organisms, hemorrhagic toxins from snake venoms, and thermolysin from bacteria.
Meanwhile, thermolysin (50 mg/mL; Sigma, USA) was also used to digest intestine tissues for comparison.
Fuji-type landscape: Application to prolyl endopeptidase and thermolysin," Biopolymers, vol.
Wu, "Effect of sonication on thermolysin hydrolysis of ovotransferrin," Food Chemistry, vol.
Yoshikawa, "Peptide inhibitors for angiotensin i-converting enzyme from thermolysin digest of dried bonitot," Bioscience, Biotechnology, and Biochemistry, vol.
Bladder biopsies were cut into small pieces and incubated overnight at 4[degrees]C in solution containing 500 mg/mL thermolysin (Sigma).
Quantitation of energy transfer between tryptophan and terbium(III) or europium(III) in thermolysin," Biochemical and Biophysical Research Communications, vol.
Wasserman, "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 Physiology, vol.
Some proteases such as pepsin and pronase are able to inactivate LPO by proteolysis but chymotrypsin did it very slowly and trypsin and thermolysin are not active against LPO [19].
PK was replaced by a metalloproteinase thermolysin, which was shown to readily digest [PrP.sup.C] into small fragments while leaving [PrP.sup.Sc] intact [48, 49].