Question

thermal deactivation​

Answer 1

Explanation:

Thermal deactivation and recovery. Enzyme deactivation was observed by heating luciferase solution to a given temperature and recording luminescence that represents the number of active enzyme molecules in solution over time.

Answer 2

Answer:

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The kinetics of enzyme deactivation provide useful insights on processes that determine the level of biological function of any enzyme. Photinus pyralis (firefly) luciferase is a convenient enzyme system for studying mechanisms and kinetics of enzyme deactivation, refolding, and denaturation caused by various external factors, physical or chemical by nature. In this report we present a study of luciferase deactivation caused by increased temperature (i.e., thermal deactivation). We found that deactivation occurs through a reversible intermediate state and can be described by a Transient model that includes active and reversibly inactive states. The model can be used as a general framework for analysis of complex, multiexponential transient kinetics that can be observed for some enzymes by reaction progression assays. In this study the Transient model has been used to develop an analytical model for studying a time course of luciferase deactivation. The model might be applicable toward enzymes in general and can be used to determine if the enzyme exposed to external factors, physical or chemical by nature, undergoes structural transformation consistent with thermal mechanisms of deactivation.

. INTRODUCTION

Mechanisms of enzyme deactivation by increasing temperature and various physical factors are complex and have not been completely understood. Traditionally a two-state model has been used to explain thermal deactivation of enzymes caused by denaturation [1–3]. The two-state model postulates an active enzyme form that irreversibly transforms into a denatured form upon heating. Yet, various experimental data show that the effect of temperature on enzymes cannot be adequately explained in terms of a two-state model that assigns the decrease of enzyme activity to irreversible denaturation [4–5]. The possibility for reversible enzyme denaturation has been discussed and recently an Equilibrium Model has been proposed to provide a quantitative explanation of the thermal behavior of enzymes [6–9].

Explanation:

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