Thermostability at ultrahigh temperatures of thermolysin and a protease from a psychrotrophic Pseudomonas.
Thermal inactivation at 110-150 degrees C of thermolysin (EC 3.4.24.4), produced by the thermophile Bacillus thermoproteolyticus, and the extracellular protease of Pseudomonas sp. MC60 a psychotroph, were investigated at 130 degrees C, both enzymes had approximately the same deltaH (22 kcal/mol) and deltaS (-13.5 cal/mol per degree) values. Both enzymes contain zinc and calcium. The amino acid compositions of the enzymes were similar except that MC60 protease exhibited a more typical tyrosine content. Comparable heat resistance at extreme temperatures of enzyme produced by psychrotrophic and thermophilic organisms emphasizes the difference between molecular properties that resist denaturation at elevated temperatures and those that allow reversible denaturation.
D000596:Amino Acids / Q000032:analysis; D002118:Calcium / Q000032:analysis; D002151:Calorimetry; D004355:Drug Stability; D004492:Edetic Acid; D006358:Hot Temperature; D008970:Molecular Weight; D010447:Peptide Hydrolases / Q000378:metabolism; D011549:Pseudomonas / Q000201:enzymology*; D013816:Thermodynamics; D013820:Thermolysin / Q000378:metabolism; D015032:Zinc / Q000032:analysis
D000596:Amino Acids; D004492:Edetic Acid; D010447:Peptide Hydrolases; D013820:Thermolysin; D015032:Zinc; D002118:Calcium