ArticleJournal of biotechnology2022
Foam fractionation of a recombinant biosurfactant apolipoprotein.
Article in Journal of biotechnology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
6 citing papers in PubMed, 13 citations in OpenAlex.
- Microbial Biofertilizers for Salinity Stress Mitigation in Hydroponic Systems.Current issues in molecular biology · 2025Review
- Biosurfactants as novel antibiofilm agents: mechanisms, biomedical applications, and applications in biofilm-associated infections.Archives of microbiology · 2025Review
- Foam Fractionation as an Efficient Method for the Separation and Recovery of Surfactants and Surface-Inactive Agents: State of the Art.ACS omega · 2025Review
- Foam fractionation studies of recombinant human apolipoprotein A-I.Biochimica et biophysica acta. Biomembranes · 2024Article
- Isolation of recombinant apolipoprotein E4 N-terminal domain by foam fractionation.Protein expression and purification · 2023Article
- Model for Investigating Relationships between Surfactant Micropollutant Properties and Their Separation from Liquid in a Bubble Column.ACS omega · 2023Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Locusta migratoria apolipophorin III (apoLp-III) possesses the ability to exist as a water soluble amphipathic α-helix bundle and a lipid surface seeking apolipoprotein. The intrinsic ability of apoLp-III to transform phospholipid vesicles into reconstituted discoidal high-density lipoproteins (rHDL) has led to myriad applications. To improve the yield of recombinant apoLp-III, studies were performed in a bioreactor. Induction of apoLp-III expression generated a protein product that is secreted from E. coli into the culture medium. Interaction of apoLp-III with gas and liquid components in media produced large quantities of thick foam. A continuous foam fractionation process yielded a foamate containing apoLp-III as the sole major protein component. The yield of recombinant apoLp-III was ~0.2 g / liter bacterial culture. Mass spectrometry analysis verified the identity of the target protein and indicated no modifications or changes to apoLp-III occurred as a result of foam fractionation. The functional ability of apoLp-III to induce rHDL formation was evaluated by incubating foam fractionated apoLp-III with phosphatidylcholine vesicles. FPLC size exclusion chromatography revealed a single major population of particles in the size range of rHDL. The results described offer a novel approach to bioreactor-based apoLp-III production that takes advantage of its intrinsic biosurfactant properties.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.