Single-step unimolecular non-first-order enzyme deactivation kinetics.

Abstract:

: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, alpha(1), and increase the first-order inactivation rate constant, k(1). The effect of protecting agents would be to increase alpha(1) and to decrease k(1).

journal_name

Biotechnol Bioeng

authors

Sadana A,Henley JP

doi

10.1002/bit.260300604

subject

Has Abstract

pub_date

1987-10-20 00:00:00

pages

717-23

issue

6

eissn

0006-3592

issn

1097-0290

journal_volume

30

pub_type

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