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Efficient preservation and breakup of liquid sheets using screen-projected particles.

ABSTRACT: In this paper, we propose a technique that can efficiently express the preservation and breakup of liquid sheets by eliminating over-preserved liquid sheets using the motion of water particles projected onto the screen. First, we project three-dimensional water particles onto a two-dimensional screen. When multiple particles are projected onto the same pixel, we select one of the front most particles as a screened particle by comparing their depth values. Based on the anisotropic kernel and density, the motion of the screened water particles is tracked to determine whether preservation and breakup should be performed. As a result, new water particles are added or existing ones are deleted, which makes it possible to express two characteristics of particle-based fluids: preservation and breakup of liquid sheets. The proposed technique is based on particle-based fluids, which can be used to remove the over-preserved liquid sheets and thus improve the quality of liquid sheets without surface noise.

SUBMITTER: Kim JH

PROVIDER: S-EPMC7001942 | biostudies-literature | 2020

REPOSITORIES: biostudies-literature

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Efficient preservation and breakup of liquid sheets using screen-projected particles.

Kim Jong-Hyun JH Lee Jung J

PloS one 20200205 2

In this paper, we propose a technique that can efficiently express the preservation and breakup of liquid sheets by eliminating over-preserved liquid sheets using the motion of water particles projected onto the screen. First, we project three-dimensional water particles onto a two-dimensional screen. When multiple particles are projected onto the same pixel, we select one of the front most particles as a screened particle by comparing their depth values. Based on the anisotropic kernel and dens ...[more]

PMID: 32023259

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Project description:Immobilized metal affinity chromatography (IMAC) is a popular and valuable method for the affinity purification of polyhistidine-tagged recombinant proteins. However, it often shows practical limitations, which might require cumbersome optimizations, additional polishing, and enrichment steps. Here, we present functionalized corundum particles for the efficient, economical, and fast purification of recombinant proteins in a column-free format. The corundum surface is first derivatized with the amino silane APTES, then EDTA dianhydride, and subsequently loaded with nickel ions. The Kaiser test, well known in solid-phase peptide synthesis, was used to monitor amino silanization and the reaction with EDTA dianhydride. In addition, ICP-MS was performed to quantify the metal-binding capacity. His-tagged protein A/G (PAG), mixed with bovine serum albumin (BSA), was used as a test system. The PAG binding capacity was around 3 mg protein per gram of corundum or 2.4 mg per 1 mL of corundum suspension. Cytoplasm obtained from different E. coli strains was examined as examples of a complex matrix. The imidazole concentration was varied in the loading and washing buffers. As expected, higher imidazole concentrations during loading are usually beneficial when higher purities are desired. Even when higher sample volumes, such as one liter, were used, recombinant protein down to a concentration of 1 µg/mL could be isolated selectively. Comparing the corundum material with standard Ni-NTA agarose beads indicated higher purities of proteins isolated using corundum. His6-MBP-mSA2, a fusion protein consisting of monomeric streptavidin and maltose-binding protein in the cytoplasm of E. coli, was purified successfully. To show that this method is also suitable for mammalian cell culture supernatants, purification of the SARS-CoV-2-S-RBD-His8 expressed in human Expi293F cells was performed. The material cost of the nickel-loaded corundum material (without regeneration) is estimated to be less than 30 cents for 1 g of functionalized support or 10 cents per milligram of isolated protein. Another advantage of the novel system is the corundum particles' extremely high physical and chemical stability. The new material should be applicable in small laboratories and large-scale industrial applications. In summary, we could show that this new material is an efficient, robust, and cost-effective purification platform for the purification of His-tagged proteins, even in challenging, complex matrices and large sample volumes of low product concentration.

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Efficient preservation and breakup of liquid sheets using screen-projected particles.

Publications

Efficient preservation and breakup of liquid sheets using screen-projected particles.

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