Design sensitivity and mixing uniformity of a micro-fluidic mixe
dc.contributor.author | Ivorra, Benjamín Pierre Paul | |
dc.contributor.author | López Redondo, Juana | |
dc.contributor.author | Ramos Del Olmo, Ángel Manuel | |
dc.contributor.author | Santiago, Juan G. | |
dc.date.accessioned | 2023-06-18T06:49:21Z | |
dc.date.available | 2023-06-18T06:49:21Z | |
dc.date.issued | 2016 | |
dc.description.abstract | We consider a particular hydrodynamic focusing microfluidic mixer used to initiate the folding process of individual proteins, which has been designed in a previous work and exhibited a mixing time of 0.1 μs. The aim of the current paper is twofold. First, we explore the sensitivity of mixing time to key geometric and flow parameters. In particular, we study the angle between inlets, the shape of the channel intersections, channel widths, mixer depth, mixer symmetry, inlet velocities, working fluid physical properties, and denaturant concentration thresholds. Second, we analyze the uniformity of mixing times as a function of inlet flow streamlines. We find the shape of the intersection, channel width, inlet velocity ratio, and asymmetries have strong effects on mixing time; while inlet angles, mixer depth, fluid properties, and concentration thresholds have weaker effects. Also, the uniformity of the mixing time is preserved for most of the inlet flow and distances of down to within about 0.4 μm of the mixer wall. We offer these analyses of sensitivities to imperfections in mixer geometry and flow conditions as a guide to experimental efforts which aim to fabricate and use these types of mixers. Our study also highlights key issues and provides a guide to the optimization and practical design of other microfluidic devices dependent on both geometry and flow conditions. | |
dc.description.department | Depto. de Análisis Matemático y Matemática Aplicada | |
dc.description.faculty | Fac. de Ciencias Matemáticas | |
dc.description.refereed | TRUE | |
dc.description.sponsorship | Ministerio de Ciencia e Innovación (MICINN) | |
dc.description.sponsorship | Junta de Andalucía | |
dc.description.sponsorship | European Regional Development Fund (ERDF) | |
dc.description.sponsorship | Universidad Complutense de Madrid | |
dc.description.sponsorship | Banco de Santander | |
dc.description.status | pub | |
dc.eprint.id | https://eprints.ucm.es/id/eprint/35214 | |
dc.identifier.doi | 10.1063/1.4939006 | |
dc.identifier.issn | 1070-6631 | |
dc.identifier.officialurl | http://scitation.aip.org/content/aip/journal/pof2/28/1/10.1063/1.4939006 | |
dc.identifier.relatedurl | http://scitation.aip.org | |
dc.identifier.uri | https://hdl.handle.net/20.500.14352/24307 | |
dc.issue.number | 1 | |
dc.journal.title | Physics of fluids | |
dc.language.iso | eng | |
dc.page.final | 012005 | |
dc.publisher | AIP Publishing | |
dc.relation.projectID | MTM2011-22658 | |
dc.relation.projectID | TIN2012-37483 | |
dc.relation.projectID | P10-TIC-6002 | |
dc.relation.projectID | P11-TIC-7176 | |
dc.relation.projectID | P12-TIC30 | |
dc.relation.projectID | Research group MOMAT (Reference No. 910480) | |
dc.rights.accessRights | open access | |
dc.subject.cdu | 532.5 | |
dc.subject.ucm | Hidrodinámica | |
dc.subject.unesco | 3301.12 Hidrodinámica | |
dc.title | Design sensitivity and mixing uniformity of a micro-fluidic mixe | |
dc.type | journal article | |
dc.volume.number | 28 | |
dcterms.references | J. Dunbar, H. P. Yennawar, S. Banerjee, J. Luo, and G. K. Farber, “The effect of denaturants on protein structure,” Protein Sci. 6(8), 1727–1733 (1997). J. A. Infante, B. Ivorra, A. M. Ramos, and J. M. Rey, “On the modeling and simulation of high pressure processes and inactivation of enzymes in food engineering,” Math. Models Methods Appl. Sci. 19(12), 2203–2229 (2009). J. P. Brody, P. Yager, R. E. Goldstein, and R. H. Austin, “Biotechnology at low reynolds numbers,” Biophys. J. 71(6),3430–3441 (1996). B. Ivorra, J. L. Redondo, J. G. Santiago, P. M. Ortigosa, and A. M. Ramos, “Two- and three-dimensional modeling and optimization applied to the design of a fast hydrodynamic focusing microfluidic mixer for protein folding,” Phys. Fluids 25(3), 1–17 (2013). D. E. Hertzog, B. Ivorra, B. Mohammadi, O. Bakajin, and J. G. Santiago, “Optimization of a microfluidic mixer for studying protein folding kinetics,” Anal. Chem. 78(13), 4299–4306 (2006). D. E. Hertzog, X. Michalet, M. Jäger, X. Kong, J. G. Santiago, S. Weiss, and O. Bakajin, “Femtomole mixer for microsecond kinetic studies of protein folding,” Anal. Chem. 76(24), 7169–7178 (2004). S. Yao and O. Bakajin, “Improvements in mixing time and mixing uniformity in devices designed for studies of proteins folding kinetics,” Anal. Chem. 79(1), 5753–5759 (2007). B. Ivorra, B. Mohammadi, J. G. Santiago, and D. E. Hertzog, “Semi-deterministic and genetic algorithms for global optimization of microfluidic protein folding devices,” Int. J. Numer. Method Eng. 66(2), 319–333 (2006). B. Ivorra, A. M. Ramos, and B. Mohammadi, “Semideterministic global optimization method: Application to a control problem of the burgers equation,” J. Optim. Theory Appl. 135(3), 549–561 (2007). B. Ivorra, B. Mohammadi, and A. M. Ramos, “Optimization strategies in credit portfolio management,” J. Global Optim. 43(2), 415–427 (2009). J. L. Redondo, J. Fernández, I. García, and P. M. Ortigosa, “A robust and efficient global optimization algorithm for planar competitive location problems,” Ann. Oper. Res. 167(1), 87–105 (2009). K. Kawahara and C. Tanford, “Viscosity and density of aqueous solutions of urea and guanidine hydrochloride,” J. Biol. Chem. 241(13), 3228–3232 (1966). B. Massey and J. Ward-Smith, Mechanics of Fluids, 8th ed. (Taylor & Francis, 2005). H. Y. Park, X. Qiu, E. Rhoades, J. Korlach, L. Kwok, W. R. Zipfel, W. W. Webb, and L. Pollack, “Achieving uniform mixing in a microfluidic device: Hydrodynamic focusing prior to mixing,” Anal. Chem. 78(13), 4465–4473 (2006). A. Rogacs and J. G. Santiago, “Temperature effects on electrophoresis,” Anal. Chem. 85(10), 5103–5113 (2013). S. Sato, C. J. Sayid, and D. P. Raleigh, “The failure of simple empirical relationships to predict the viscosity of mixed aqueous solutions of guanidine hydrochloride and glucose has important implications for the study of protein folding,” Protein Sci. 43(9), 1601–1603 (2000). G. Gannon, J. A. Larsson, J. C. Greer, and D. Thompson, “Guanidinium chloride molecular diffusion in aqueous and mixed water-ethanol solutions,” J. Phys. Chem. B 112(30), 8906–8911 (2008). | |
dspace.entity.type | Publication | |
relation.isAuthorOfPublication | 6d5e1204-9b8a-40f4-b149-02d32e0bbed2 | |
relation.isAuthorOfPublication | 581c3cdf-f1ce-41e0-ac1e-c32b110407b1 | |
relation.isAuthorOfPublication.latestForDiscovery | 6d5e1204-9b8a-40f4-b149-02d32e0bbed2 |
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