A series of fluorinated acrylates [F(CF 2 ) q O(CH 2 ) p OOCOCHACH 2 , where q ϭ 8 and p ϭ 2 Ϭ 11) were synthesized and used as comonomers in the photopolymerization of acrylic systems. These fluoroacrylates were synthesized in a three-step procedure through the radical addition of perfluoroalkyliodides to an unsaturated alcohol followed by their acrylation. The mixtures, containing up to 0.8% (w/w) of the comonomers, produced transparent films after UV curing; they showed changes in the surface properties as a function of the comonomer type and concentration. With contactangle and X-ray photoelectron spectroscopy analyses, the relationship between the structure of the monomers and the surface properties of the UV-cured films was investigated: the wettability decreased, depending on the length of the fluorinated group (q value) and the hydrogenated segment of the monomer (p value).
New acrylic and allylic resins were prepared by functionalising perfluoropolyethers chains, which assured peculiar surface properties. Blends having a different amount of the acrylic and of the allylic systems were cured in air by UV irradiation. The cure of the films was found dependent on the ratio between the two resins; the concentration for the obtaining of a film fully cured in air was determined. On the basis of this concentration, a macromer functionalised with the right amount of both the acrylic group and the allylic one was synthesised.
Cellulases are enzymes with great potential for converting biomass to biofuels for sustainable energy. However, their commercial use is limited by their costs and low reusability. Therefore, the scientific and industrial sectors are focusing on finding better strategies to reuse enzymes and improve their performance. In this work, cellulase from Aspergillus niger was immobilised through in situ entrapment and adsorption on bio-inspired silica (BIS) supports. To the best of our knowledge, this green effect strategy has never been applied for cellulase into BIS. In situ entrapment was performed during support synthesis, applying a one-pot approach at mild conditions (room temperature, pH 7, and water solvent), while adsorption was performed after support formation. The loading efficiency was investigated on different immobilisation systems by Bradford assay and FTIR. Bovine serum albumin (BSA) was chosen as a control to optimize cellulase loading. The residual activity of cellulase was analysed by the dinitro salicylic acid (DNS) method. Activity of 90% was observed for the entrapped enzyme, while activity of ~55% was observed for the adsorbed enzyme. Moreover, the supported enzyme systems were recycled five times to evaluate their reuse potential. The thermal and pH stability tests suggested that both entrapment and adsorption strategies can increase enzyme activity. The results highlight that the entrapment in BIS is a potentially useful strategy to easily immobilise enzymes, while preserving their stability and recycle potential.
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