Chemotactic Separation of Enzymes
Citations Over TimeTop 10% of 2014 papers
Abstract
We demonstrate a procedure for the separation of enzymes based on their chemotactic response toward an imposed substrate concentration gradient. The separation is observed within a two-inlet, five-outlet microfluidic network, designed to allow mixtures of active (ones that catalyze substrate turnover) and inactive (ones that do not catalyze substrate turnover) enzymes, labeled with different fluorophores, to flow through one of the inlets. Substrate solution prepared in phosphate buffer was introduced through the other inlet of the device at the same flow rate. The steady-state concentration profiles of the enzymes were obtained at specific positions within the outlets of the microchannel using fluorescence microscopy. In the presence of a substrate concentration gradient, active enzyme molecules migrated preferentially toward the substrate channel. The excess migration of the active enzyme molecules was quantified in terms of an enrichment coefficient. Experiments were carried out with different pairs of enzymes. Coupling the physics of laminar flow of liquid and molecular diffusion, multiphysics simulations were carried out to estimate the extent of the chemotactic separation. Our results show that, with appropriate microfluidic arrangement, molecular chemotaxis leads to spontaneous separation of active enzyme molecules from their inactive counterparts of similar charge and size.
Related Papers
- → Thermal management of electronic components based on hierarchical microchannels and nanofluids(2023)25 cited
- → Flow distribution in microchannel devices with U-shaped manifolds(2023)13 cited
- → Effects of microchannel geometry on preconcentration intensity in microfluidic chips with straight or convergent–divergent microchannels(2012)20 cited
- → Direct Chemotaxis and Leucocyte‐Induced Chemotaxis of Polymorphonuclear Leucocytes(1978)15 cited
- STUDIES ON MICROFLUID FLOW CONTROLS BASED ON THE CONFIGURATION OF MICROCHANNEL(2009)