Thermal inactivation kinetics of penicillin g acylase obtained from a mutant derivative of escherichia coli atcc 11105

Thermal inactivation kinetics of native and glutaraldehyde cross‐linked forms of penicillin G acylase obtained from a mutant derivative of Escherichia coli ATCC 11105 were studied. Apparent activation energies for thermal inactivation of both native and cross‐linked forms of enzyme were calculated to be [57‐71 ± 8.46] and [67.11 ± 13.83] kcal mol −1 respectively. This slight increase in activation energy‐suggested that glutaraldehyde cross‐linking did not markedly protect against thermal inactivation. Cross‐linked enzyme did, however, have a significantly improved half‐life at temperatures between 40°C and 50°C.