Encyclopedia of Bioprocess Technology - Fermentation, by Michael C. Flickinger, Stephen W. Drew

By Michael C. Flickinger, Stephen W. Drew

Encyclopedias composed of: The Encyclopedia of Molecular Biology, the Encyclopedia of Bioprocess know-how: Fermentation, Biocatalysis, and Bioseparation, the Encyclopedia of phone know-how, and the Encyclopedia of moral, criminal, and coverage concerns in Biotechnology, offering wide assurance of 4 significant modern issues during this box. DLC: Biochemical engineering--Encyclopedias.

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Henderson, N. Mehta, C. H. Botting, L. Pocivavsek, C. A. Fierke, E. J. Toone, and J. H. Naismith, Directed evolution of a new catalytic site in 2-keto-3-deoxy-6phosphogluconate aldolase from Escherichia coli, Structure 2001, 9, 1–10. A. Zaks, Industrial biocatalysis, Curr. Opin. Chem. Biol. 2001, 5, 130–136. 19 2 Characterization of a (Bio-)catalyst Summary Enzymes are a class of macromolecules with the ability both to bind small molecules and to effect reaction. Stabilizing forces such as hydrophobic effects only slightly dominate destabilizing forces such as Coulombic forces of equal polarity; thus the Gibbs free enthalpy of formation of proteins, ∆Gformation, is only weakly negative.

Storage stability over time under fixed conditions of temperature, pH value and concentration of additives often can be expressed by a first-order decay law (analogous to radioactive decay) [Eq. 19)]. 19) The validity of a first-order decay law over time for the activity of enzymes according to Eq. 19), with [E]t and [E]0 as the active enzyme concentration at time t or 0, respectively, and kd as the deactivation rate constant, is based on the suitability of thinking of the deactivation process of enzymes in terms of Boltzmann statistics.

In this context, enzymes are often referred to as “entropy traps”, because many contributions to entropy are “frozen in” after binding of the substrate to the enzyme molecule. y Many enzymatic reaction mechanisms are accelerated or even only made possi- ble by the absence of water or other solvents. The enzyme supports desolvation by redirecting part of the possible binding energy liberated from the binding between enzyme and substrate. 2 Sources and Reasons for the Activity of Enzymes as Catalysts The upper boundary of the reaction rate is reached when every collision between substrate and enzyme molecules leads to reaction and thus to product.

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