Ammann, Erik

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Ammann
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Erik
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Ammann, Erik

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2016 - 201912020 - 20232
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  • Vorschaubild nicht verfügbar
    Publikation
    Leaching of dissolved organic carbon from commercial reverse osmosis membranes exacerbates interferences in organic solute rejection during bench-scale filtration
    (Elsevier, 15.03.2023) Li, Zhao; Orlando, Adriano; Müller, Sarah I.; Ammann, Erik; Ding, An; Desmond, Peter [in: Desalination]
    01A - Beitrag in wissenschaftlicher Zeitschrift
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    Publikation
    Low-Temperature Reactive Aerosol Processing for Large-Scale Synthesis of Selenium Nanoparticles
    (American Chemical Society, 22.08.2020) Viacava, Karen; Ammann, Erik; Lenz, Markus [in: Industrial & Engineering Chemistry Research]
    Selenium nanoparticles (SeNPs) have been suggested for various applications such as food, animal feed, and biomedicine. However, thus far, wet chemical synthesis cannot produce sufficient quantities of SeNPs at the required quality. In this study, reactive aerosol processing is employed to produce SeNPs as powder concentrates of 2.2 to 4.0% (dry weight basis) on the scale of hundreds of kilograms. Citric acid is the most efficient organic precursor (92.5% SeNPs), but polydisperse particles are obtained, and some unknown dissolved Se species are present in the final product. Glycine is less efficient (82.2% SeNPs); however, monodisperse nanoparticles (153 nm; D90 = 215 nm) are obtained, with selenite being the only residue in the final product. The obtained particles consisted of X-ray amorphous (i.e., not diffracting) Se, since no elemental Se allotrope or other solid Se phases were indicated in X-ray diffraction. Reactive aerosol processing involves a limited number of preparation steps (i.e., dissolution and atomization), uses only food-/feed-approved ingredients (selenite, citric acid, glycine) and allows continuous operation and zero waste generation. This makes reactive aerosol processing ideal for the large-scale production of SeNPs.
    01A - Beitrag in wissenschaftlicher Zeitschrift
  • Vorschaubild nicht verfügbar
    Publikation
    Production of superparamagnetic nanobiocatalysts for green chemistry applications
    (Springer, 23.04.2016) Gasser, Christoph; Ammann, Erik; Schäffer, Andreas; Shahgaldian, Patrick; Corvini, Philippe [in: Applied Microbiology and Biotechnology]
    Immobilization of enzymes on solid supports is a convenient method for increasing enzymatic stability and enabling enzyme reuse. In the present work, a sorption-assisted surface conjugation method was developed and optimized to immobilize enzymes on the surface of superparamagnetic nanoparticles. An oxidative enzyme, i.e., laccase from Trametes versicolor was used as model enzyme. The immobilization method consists of the production of superparamagnetic nanoparticles by co-precipitation of FeCl2 and FeCl3. Subsequently, the particle surface is modified with an organosilane containing an amino group. Next, the enzymes are adsorbed on the particle surface before a cross-linking agent, i.e., glutaraldehyde is added which links the amino groups on the particle surface with the amino groups of the enzymes and leads to internal cross-linking of the enzymes as well. The method was optimized using response surface methodology regarding optimal enzyme and glutaraldehyde amounts, pH, and reaction times. Results allowed formulation of biocatalysts having high specific enzymatic activity and improved stability. The biocatalysts showed considerably higher stability compared with the dissolved enzymes over a pH range from 3 to 9 and in the presence of several chemical denaturants. To demonstrate the reusability of the immobilized enzymes, they were applied as catalysts for the production of a phenoxazinone dye. Virtually, 100 % of the precursor was transformed to the dye in each of the ten conducted reaction cycles while on average 84.5 % of the enzymatic activity present at the beginning of a reaction cycle was retained after each cycle highlighting the considerable potential of superparamagnetic biocatalysts for application in industrial processes.
    01A - Beitrag in wissenschaftlicher Zeitschrift