Studying solutions at high shear rates: a dedicated microfluidics setup

Wieland, D. C. Florian; Garamus, V. M.; Zander, Thomas; Krywka, Christina; Wang, M.; Dédinaité, Andra; Claesson, Per M.; Willumeit‐Römer, Regine

doi:10.1107/s1600577515024856

Cited by 12 publications

(11 citation statements)

References 50 publications

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“…Harrington et al immobilized penicillinase and lactate dehydrogenase on the inner wall of a nylon tube and stressed these proteins with shear rates up to 10 350 s −1 without any loss in activity. Although this is not extraordinarily high compared to our work or other studies, the applied shear force could not be transferred to rotate proteins; thus, the proteins sensed maximum shear rates at any time. However, as already described, the force required to unfold a protein was measured by atomic force microscopy to be near 20 and 220 pN for an alpha‐helical and beta sheet dominated protein, respectively.…”

Section: Resultscontrasting

confidence: 57%

Impact of Cavitation, High Shear Stress and Air/Liquid Interfaces on Protein Aggregation

Duerkop

Berger

Dürauer

et al. 2018

Biotechnology Journal

102

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The reported impact of shear stress on protein aggregation has been contradictory. At high shear rates, the occurrence of cavitation or entrapment of air is reasonable and their effects possibly misattributed to shear stress. Nine different proteins (α-lactalbumin, two antibodies, fibroblast growth factor 2, granulocyte colony stimulating factor [GCSF], green fluorescence protein [GFP], hemoglobin, human serum albumin, and lysozyme) are tested for their aggregation behavior on vapor/liquid interfaces generated by cavitation and compared it to the isolated effects of high shear stress and air/liquid interfaces generated by foaming. Cavitation induced the aggregation of GCSF by þ68.9%, hemoglobin þ4%, and human serum albumin þ2.9%, compared to a control, whereas the other proteins do not aggregate. The protein aggregation behaviors of the different proteins at air/liquid interfaces are similar to cavitation, but the effect is more pronounced. Air-liquid interface induced the aggregation of GCSF by þ94.5%, hemoglobin þ35.5%, and human serum albumin (HSA) þ31.1%.The results indicate that the sensitivity of a certain protein toward cavitation is very similar to air/liquid-induced aggregation. Hence, hydroxyl radicals cannot be seen as the driving force for protein aggregation when cavitation occurs. Further, high shear rates of up to 10 8 s À1 do not affect any of the tested proteins. Therefore, also within this study generated extremely high isolated shear rates cannot be considered to harm structural integrity when processing proteins.

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Section: Resultscontrasting

confidence: 57%

Impact of Cavitation, High Shear Stress and Air/Liquid Interfaces on Protein Aggregation

Duerkop

Berger

Dürauer

et al. 2018

Biotechnology Journal

102

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show abstract

“…3). Although studies on high shear rate-dependent aggregation have been reported [5,9,[32][33][34][35], the values from our simulation exceed these values by a factor of at least 10. In addition, the maximum shear rate was 22-times higher than one would expect from the laminar flow profile at the wall (4.5 × 10 6 s −1 ), which further indicates the importance of a validated CFD simulation.…”

Section: Cfd Simulation Of Shear Ratescontrasting

confidence: 82%

Influence of cavitation and high shear stress on HSA aggregation behavior

Duerkop

Berger

Dürauer

et al. 2017

Engineering in Life Sciences

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Neither the influence of high shear rates nor the impact of cavitation on protein aggregation is fully understood. The effect of cavitation bubble collapse‐derived hydroxyl radicals on the aggregation behavior of human serum albumin (HSA) was investigated. Radicals were generated by pumping through a micro‐orifice, ultra‐sonication, or chemically by Fenton's reaction. The amount of radicals produced by the two mechanical methods (0.12 and 11.25 nmol/(L min)) was not enough to change the protein integrity. In contrast, Fenton's reaction resulted in 382 nmol/(L min) of radicals, inducing protein aggregation. However, the micro‐orifice promoted the formation of soluble dimeric HSA aggregates. A validated computational fluid dynamic model of the orifice revealed a maximum and average shear rate on the order of 108 s−1 and 1.2 × 106 s−1, respectively. Although these values are among the highest ever reported in the literature, dimer formation did not occur when we used the same flow rate but suppressed cavitation. Therefore, aggregation is most likely caused by the increased surface area due to cavitation‐mediated bubble growth, not by hydroxyl radical release or shear stress as often reported.

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“…Poiseuille flow geometries, to perform structural rheology experiments, [18][19][20] allowing access to high shear rates in the regime ofγ ≈ 10 5 − 10 6 s −1 . 21 These shear rates correspond to the regime where structural modulations due to shear are expected. 2 By this approach, structural response of soft matter systems on shear can be studied with high spatial resolution.…”

mentioning

confidence: 98%

Microsecond Structural Rheology

Lehmkühler

Steinke

Schroer

et al. 2017

J. Phys. Chem. Lett.

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The relationship between the local structure of complex liquids and their response to shear is generally not well understood. This concerns, in particular, the formation of particle strings in the flow direction or hydroclusters, both important for the understanding of shear thinning and thickening phenomena. Here, we present results of a microfocus X-ray scattering experiment on spherical silica colloids in a liquid jet at high shear rates. Along and across the jet, we observe direction-dependent modifications of the structure factor of the suspension, suggesting the formation of differently ordered clusters in compression lines and as particle strings. With increasing distance from the orifice, the structure relaxes to the unsheared case with a typical relaxation 10 times larger as the time scale of Brownian motion. These results provide the first experimental flow characterization of a complex fluid at high shear rates detecting cluster formation and relaxation with micrometer and microsecond resolution.

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Studying solutions at high shear rates: a dedicated microfluidics setup

Cited by 12 publications

References 50 publications

Impact of Cavitation, High Shear Stress and Air/Liquid Interfaces on Protein Aggregation

Impact of Cavitation, High Shear Stress and Air/Liquid Interfaces on Protein Aggregation

Influence of cavitation and high shear stress on HSA aggregation behavior

Microsecond Structural Rheology

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