Enzymatic reactions in microfluidic devices: Michaelis-Menten kinetics

William D. Ristenpart, Jiandi Wan, Howard A. Stone

Research output: Contribution to journalArticle

48 Scopus citations

Abstract

Kinetic rate constants for enzymatic reactions are typically measured with a series of experiments at different substrate concentrations in a well-mixed container. Here we demonstrate a microfluidic technique for measuring Michaelis-Menten rate constants with only a single experiment. Enzyme and substrate are brought together in a coflow microfluidic device, and we establish analytically and numerically that the initial concentration of product scales with the distance x along the channel as x5/2. Measurements of the initial rate of product formation, combined with the quasi-steady rate of product formation further downstream, yield the rate constants. We corroborate the x5/2 scaling result experimentally using the bioluminescent reaction between ATP and luciferase/luciferin as a model system.

Original languageEnglish (US)
Pages (from-to)3270-3276
Number of pages7
JournalAnalytical Chemistry
Volume80
Issue number9
DOIs
StatePublished - May 1 2008

All Science Journal Classification (ASJC) codes

  • Analytical Chemistry

Fingerprint Dive into the research topics of 'Enzymatic reactions in microfluidic devices: Michaelis-Menten kinetics'. Together they form a unique fingerprint.

  • Cite this