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Single‐step unimolecular non‐first‐order enzyme deactivation kinetics
Author(s) -
Sadana Ajit,
Henley James P.
Publication year - 1987
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260300604
Subject(s) - kinetics , chemistry , enzyme , ionic strength , acetylcholinesterase , enzyme kinetics , reaction rate constant , first order , biophysics , stereochemistry , active site , biochemistry , organic chemistry , biology , mathematics , physics , quantum mechanics , aqueous solution
A two‐parameter deactivation model is proposed to describe the kinetics of activity stabilization for some enzymes. The single‐step unimolecular mechanism exhibits non‐first‐order deactivation kinetics since the final enzyme state, E 1 is not completely inactivated. The usefulness of the model is demonstrated by applying it to the inactivation of different enzymes. The influence of the concentration of active ester, ionic strength, and pH on the model parameters is examined during the inactivation of electric eel acetylcholinesterase. 25 In general, inactivators would decrease the level of activity stabilization, α 1 , and increase the first‐order inactivation rate constant, k 1 . The effect of protecting agents would be to increase α 1 and to decrease k 1 .