Experimental approaches to a better understanding of mixing performance of microfluidic devices

Panić, Slobodan; Loebbecke, S.; Tuercke, T.; Antes, J.; Bošković, D.

doi:10.1016/j.cej.2003.10.026

Cited by 148 publications

(106 citation statements)

References 7 publications

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“…To characterize the mixing performance of the micromixers in order to better understand and design more efficient micromixers for different applications, a number of techniques, both experimentally [14][15][16][17][18] and theoretically [12,[19][20][21][22][23][24][25][26][27][28], have been employed. Particularly, CFD has been widely used to study the mixing behavior of micromixers in details.…”

Section: Open Accessmentioning

confidence: 99%

Evaluation of Floor-grooved Micromixers using Concentration-channel Length Profiles

Zhang

Yim

et al. 2010

Micromachines

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Abstract:We evaluated the dynamic micromixing performances in slanted groove micromixers (SGM) and staggered herringbone micromixers (SHM) and quantitatively compared their differences using concentration vs. channel length profiles obtained from numerical stimulations. It is found that faster and finer mixing took place in the SHM and the chaotic mixing was more effective at locations closer to the grooves; in comparison, slower and coarser mixing occurred throughout the whole channel of the SGM. Subsequently, the concentration profile-based characterization method was demonstrated in hybrid floor-grooved micromixers to study the interaction of SGM and SHM.

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Section: Open Accessmentioning

confidence: 99%

Evaluation of Floor-grooved Micromixers using Concentration-channel Length Profiles

Zhang

Yim

et al. 2010

Micromachines

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“…[29][30][31] In most cases, the best definition of mixing time is an ad hoc rule that takes into account the figures of merit of a specific application. We here propose a mixing definition for our mixer that well characterizes the temporal resolution of subsequent macromolecular folding kinetics measurements.…”

Section: Definition Of Mixing Timementioning

confidence: 99%

Femtomole Mixer for Microsecond Kinetic Studies of Protein Folding

et al. 2004

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We have developed a microfluidic mixer for studying protein folding and other reactions with a mixing time of 8 μs and sample consumption of femtomoles. This device enables us to access conformational changes under conditions far from equilibrium and at previously inaccessible time scales. In this paper, we discuss the design and optimization of the mixer using modeling of convective diffusion phenomena and a characterization of the mixer performance using microparticle image velocimetry, dye quenching, and Förster resonance energy-transfer (FRET) measurements of single-stranded DNA. We also demonstrate the feasibility of measuring fast protein folding kinetics using FRET with acyl-CoA binding protein.In protein folding, important structural events occur on a microsecond time scale. 1 To study their kinetics, folding reactions must be initiated at even shorter time scales. Photochemical initiation 2 and changes in temperature, 3 pressure, 4,5 or chemical potential, as in salt or chemical denaturant concentration changes, 6-9 all provide the perturbation of protein conformational equilibria necessary to initiate folding. Laser temperature-jump relaxation provides the best temporal resolution with dead times in the nanosecond range, 3 but only a small number of proteins denature reversibly at elevated temperature. Temperature-jump techniques are also limited to conditions near the equilibrium unfolding transition where marginally stable folding intermediates are less likely to accumulate. Pressure relaxation initiates the folding process by exploiting a change in the volume between the folded and unfolded conformers. Pressure changes up to 20 MPa in under 100 μs have been created with piezoelectric devices to monitor rate-limiting barrier crossing in the cold shock protein with Förster resonance energy transfer (FRET). 10 However, in pressure-jump experiments, the folding equilibrium is shifted only marginally at low denaturant concentrations where collapse occurs, and chain collapse is therefore not easily measured via FRET as refolding amplitudes are small. 10-12In comparison to temperature-and pressure-jump relaxation techniques, folding experiments based on changes in chemical potential, via rapid mixing of protein solutions in to and out of chaotrope solvents, are more versatile. The technique is applicable to a wide range of proteins as most unfold reversibly in the presence of chemical denaturants such as urea 7 and guanidine hydrochloride (GdCl). 6 Further, mixer-based experiments are not limited to proteins near the folding transition state. Until recently, the main limitation of mixer-based experiments was

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“…Among those are the concentration of the acid injected, 2,4 the acid feed point, 2,4,5 the acid feed time, 2,4 the geometry of the mixing accessory, 4 and the stirrer speed. 2,[4][5][6] Later, the reaction scheme was applied for characterizing mixing in continuous flow devices, 7 where two flows were combined in the device in a flow ratio of 1:1. One feed contained sulfuric acid in a rather low concentration; the other feed contained the other reactants.…”

Section: The Iodide Iodate Reaction Methodsmentioning

confidence: 99%

On the use of the Iodide Iodate Reaction Method for assessing mixing times in continuous flow mixers

Kölbl

Kraut

2011

AIChE Journal

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It is demonstrated experimentally by example of simple, commercially available T‐junctions and by ”unsymmetrical” V‐type micromixers that mixing times cannot be derived by applying the Iodide Iodate Reaction Method without considering the specific mixer geometry. Experimental results differ depending on the orientation of the feeds with respect to the inlets. An explanation for the observed effects is suggested. © 2010 American Institute of Chemical Engineers AIChE J, 2011

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Experimental approaches to a better understanding of mixing performance of microfluidic devices

Cited by 148 publications

References 7 publications

Evaluation of Floor-grooved Micromixers using Concentration-channel Length Profiles

Evaluation of Floor-grooved Micromixers using Concentration-channel Length Profiles

Femtomole Mixer for Microsecond Kinetic Studies of Protein Folding

On the use of the Iodide Iodate Reaction Method for assessing mixing times in continuous flow mixers

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