Enzymatic degradation of p-chlorophenol was carried out in a two-phase flow in a microchannel (100 microm width, 25 microm depth) fabricated on a glass plate (70 mm x 38 mm). This is the first report on the enzymatic reaction in a two-phase flow on a microfluidic device. The surface of the microchannel was partially modified with octadecylsilane groups to be hydrophobic, thus allowing clear phase separation at the end-junction of the microchannel. The enzyme (laccase), which is surface active, was solubilized in a succinic aqueous buffer and the substrate (p-chlorophenol) was in isooctane. The degradation of p-chlorophenol occurred mainly at the aqueous-organic interface in the microchannel. We investigated the effects of flow velocity and microchannel shape on the enzymatic degradation of p-chlorophenol. Assuming that diffusion of the substrate (p-chlorophenol) is the rate-limiting step in the enzymatic degradation of p-chlorophenol in the microchannel, we proposed a simple theoretical model for the degradation in the microchannel. The calculated degradation values agreed well with the experimental data.

Published online in Wiley InterScience (www.interscience.wiley.com).The purpose of the present study was to investigate fluidic behavior in a microchannel with hair-pin curves, using a three-dimensional (3-D)

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The oxidative dehydrogenation of sodium lactate to sodium pyruvate in an aqueous phase proceeded favorably using Pd/C and that doped with Te at 358 K with no adjustment in solution pH under pressurized oxygen, although previous reports had stated that this reaction would not proceed using Pd/C while Pd/C doped with either Pb, Bi or Te showed the activity at atmospheric pressure, 363 K, and a pH of 8.