Synthesis of biomass derived levulinate esters on novel sulfated Zr/KIL-2 composite catalysts

Zirconia nanomaterials were prepared by impregnation of KIL-2 type silica with 4, 8, 15 and 25 wt% of ZrO2, and were modified by sulfate groups in order to vary the type, strength and density of the active sites. The samples were characterized by X-ray powder diffraction (XRD), EDX analysis, N-2 physisorption, SEM, TEM, UV Vis spectroscopy, XPS, and thermogravimetric analysis (TGA). The acidic properties were investigated by FT-IR spectroscopy of adsorbed pyridine. The catalytic properties of ZrKIL-2 catalysts and their sulfated varieties were studied in levulinic acid (LA) esterification with ethanol or n-butanol. The sulfated materials showed significantly higher activity compared to the non-sulfated ones due to their stronger Bronsted and Lewis acid sites. It was found that the silica supported sulfated samples show different activity depending on the applied alcohol. With increasing ZrO2 content up to 15 wt% increasing catalytic activity and selectivity was observed to produce levulinate esters. A further increase of the amount of zirconia leads to a decrease in catalytic activity because of the significant decrease of ZrO2 dispersion and the structure deterioration of the catalyst. For the first time insight was provided into the relation between sulfates group leaching and zirconia dispersion. (C) 2016 Elsevier Inc. All rights reserved

Recent Progress in Synthesis and Application of Nanosized and Hierarchical Mordenite—A Short Review

Gefördert durch den Publikationsfonds der Universität Kasse

Ion-Exchanged Clinoptilolite as a Substrate for Space Farming

Clinoptilolite, with its structural peculiarities (ion-exchange and adsorbent properties), is an excellent candidate for direct use and various modifications. In this study, we explored the effect of ion exchange and the particle size of clinoptilolite on Raphanus sativus seed germination, plant growth, physiological and biochemical characteristics of plants. Plants were grown, for three consecutive runs, on non-modified clinoptilolite, 0.9–2.5 mm (C-2.5) and 2.5–5.0 mm (C-5.0); clinoptilolite fractions modified with ion exchange with ammonium (CNH4-2.5 and CNH4-5.0); and potassium (CK-2.5 and CK-5.0) ions. Our data revealed that ion exchange with ammonium increased water-holding capacity, while potassium exchange decreased the water-holding capacity of the substrates irrespective of their particle size. The positive effect of small fractions ion-exchanged clinoptilolite (CNH4-2.5 and CK-2.5) on seed germination, during the third run, was established. The small clinoptilolite fractions favored root crop production, particularly in CK-2.5 plants only during the first run. Substantial positive effect on the content of total carbohydrates and polyphenols especially during the third run was established in plants grown on potassium-exchanged clinoptilolite. Our findings support the future exploration of clinoptilolite as a suitable substrate for plant growth in space and ground-based facilities for space-oriented experiments

Effects of Ca2+ ions on bestrophin-1 surface films.

Human bestrophin-1 (hBest1) is a transmembrane calcium-activated chloride channel protein - member of the bestrophin family of anion channels, predominantly expressed in the membrane of retinal pigment epithelium (RPE) cells. Mutations in the protein cause ocular diseases, named Bestrophinopathies. Here, we present the first Fourier transform infrared (FTIR) study of the secondary structure elements of hBest1, π/A isotherms and hysteresis, Brewster angle microscopy (BAM) and atomic force microscopy (AFM) visualization of the aggregation state of protein molecules dispersed as Langmuir and Langmuir-Blodgett films. The secondary structure of hBest1 consists predominantly of 310-helices (27.2%), α-helixes (16.3%), β-turns and loops (32.2%). AFM images of hBest1 suggest approximate lateral dimensions of 100×160Å and 75Å height. Binding of calcium ions (Ca2+) induces conformational changes in the protein secondary structure leading to assembly of protein molecules and changes in molecular and macro-organization of hBest1 in monolayers. These data provide basic information needed in pursuit of molecular mechanisms underlying retinal and other pathologies linked to this protein