Thermal denaturation of native and cross-linked Bacillus cereus 569/H beta-lactamase I.
Thermal denaturation of native and internally cross-linked Bacillus cereus 569/H beta-lactamase I (beta-lactamhydrolase, EC 3.5.2.6) was investigated using differential scanning calorimetry. Application of temperature-scanning kinetics provided an estimate of various activation parameters for the denaturation process. Evidence is presented to indicate that subtle temperature-induced conformational changes preceding gross denaturation are sufficient to cause inactivation of the enzyme.
D001409:Bacillus cereus / Q000201:enzymology*; D002151:Calorimetry; D003432:Cross-Linking Reagents; D006358:Hot Temperature; D007700:Kinetics; D011489:Protein Denaturation; D013816:Thermodynamics; D001618:beta-Lactamases
D003432:Cross-Linking Reagents; D001618:beta-Lactamases