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 activation. Cross-linked enzyme did, however, have a significantly improved half-life at temperatures between 40 degrees C and 50 degrees C.
Department of Biology, Scientific and Technical Research Council of Turkey, Marmara Research Center, Gebze-Kocaeli.
A
A
Erarslan
H
H
Koçer
D003432:Cross-Linking Reagents / Q000494:pharmacology; D004789:Enzyme Activation; D004795:Enzyme Stability; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D005976:Glutaral / Q000494:pharmacology; D006358:Hot Temperature; D007700:Kinetics; D009154:Mutation; D010399:Penicillin Amidase / Q000187:drug effects / Q000378:metabolism*
D003432:Cross-Linking Reagents; D010399:Penicillin Amidase; D005976:Glutaral