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

Single-step unimolecular non-first-order enzyme deactivation kinetics. Research Abstract Details 

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Single-step unimolecular non-first-order enzyme deactivation kinetics. Abstract Text:

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).

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Single-step unimolecular non-first-order enzyme deactivation kinetics. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Biotechnology and bioengineering

VOLUME: 30

Page Numbers: 717-23

Journal Abbreviation: Biotechnol. Bioeng.

ISSN: 0006-3592

DAY: 20

MONTH: Oct

YEAR: 1987

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LANGUAGE: eng

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Grant and Affiliation Information for Single-step unimolecular non-first-order enzyme deactivation kinetics.

AFFILIATION: Chemical Engineering Department, University of Mississippi, University, MS 38677.

Country: United States

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MEDLINETA: Biotechnol Bioeng

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