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Thermal inactivation kinetics of penicillin g acylase obtained from a mutant derivative of escherichia coli atcc 11105
Author(s) -
Erarslan Altan,
Koçer Halil
Publication year - 1992
Publication title -
journal of chemical technology and biotechnology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.64
H-Index - 117
eISSN - 1097-4660
pISSN - 0268-2575
DOI - 10.1002/jctb.280550113
Subject(s) - glutaraldehyde , escherichia coli , kinetics , chemistry , mutant , penicillin , enzyme , activation energy , derivative (finance) , enzyme kinetics , nuclear chemistry , biochemistry , chromatography , active site , antibiotics , organic chemistry , gene , physics , quantum mechanics , financial economics , economics
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.