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- W1989071393 abstract "This paper reports a method to characterize the kinetic constants for the action of enzymes on immobilized substrates. This example uses cutinase, a serine esterase that hydrolyzes 4-hydroxyphenyl valerate moieties that are immobilized on a self-assembled monolayer of alkanethiolates on gold. The product of the enzyme reaction is a hydroquinone, which is redox active and therefore permits the use of cyclic voltammetry to monitor the extent of reaction in situ. A kinetic model based on the Michaelis-Menten formalism is used to analyze the dependence of initial rates of reaction on both the substrate density and the enzyme concentration. The resulting value of k(cat)/K(M) for the interfacial reaction is comparable to that for a homogeneous phase reaction with a substrate of similar structure. This strategy of using monolayers presenting substrates for the enzyme and cyclic voltammetry to measure reaction rates provides quantitative and real-time information on reaction rates and permits a level of analysis of interfacial enzyme reactions that to date has been difficult to realize." @default.
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- W1989071393 date "2007-04-03" @default.
- W1989071393 modified "2023-09-25" @default.
- W1989071393 title "Determination of Kinetic Parameters for Interfacial Enzymatic Reactions on Self-Assembled Monolayers" @default.
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- W1989071393 doi "https://doi.org/10.1021/la062860k" @default.
- W1989071393 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2518328" @default.
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