Thermal inactivation kinetics of penicillin G acylase obtained from a mutant derivative of Escherichia coli ATCC 11105.

doi:10.1002/jctb.280550113

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Article

Thermal inactivation kinetics of penicillin G acylase obtained from a mutant derivative of Escherichia coli ATCC 11105.

Journal of chemical technology and biotechnology (Oxford, Oxfordshire : 1986) - 1 Jan 1992

Erarslan A, Koçer H

Abstract excerpt

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 calculate...

Topics

Cross-Linking Reagents
Enzyme Activation
Enzyme Stability
Escherichia coli
Glutaral
Hot Temperature
Kinetics
Mutation
Penicillin Amidase

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