In situ fabrication of cross-linked protein membranes by using microfluidics.

We report a novel technique for preparing cross-linked protein membranes within microchannels by using an interfacial cross-linking reaction. Glass microchannels with a Y input were assembled by using a simple adhesive bonding technique to achieve dual, parallel laminar flows. Membrane formation utilised an interfacial reaction at the liquid-liquid interface, which involved bovine serum albumin (aqueous solution with a flow rate of 300 microL min(-1)) and terephthaloyl chloride (xylene solution with a flow rate of 700 microL min(-1)), to form thin ( approximately 25 microm) cross-linked films along the length of the channel under the continuous pressure-driven laminar flow. Such microfabricated membranes could extend the separation potential of any microfluidic structure to provide a stable barrier layer. Furthermore, degradation of the membrane was possible by using an alkali sodium dodecyl sulfate solution, which led to the complete disappearance of the membrane. These membranes could facilitate additional modification to allow for different permeability properties by controlled degradation. The one-step in situ membrane-fabrication methodology reported here generated precisely localised membranes and avoided the complexities of subcomponent assembly, which require complicated alignment of small, preformed membranes. This methodology could become the basis for sophisticated microseparation systems, biosensors and several "lab-on-a-chip" devices.