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• W2044430247 abstract "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." @default.
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• W2044430247 date "2007-04-24" @default.
• W2044430247 modified "2023-10-11" @default.
• W2044430247 title "Thermal inactivation kinetics of penicillin g acylase obtained from a mutant derivative of escherichia coli atcc 11105" @default.
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• W2044430247 doi "https://doi.org/10.1002/jctb.280550113" @default.
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