3 resultados para Study of stability

em Universidad de Alicante


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Poly(lactic acid) (PLA) was melt-blended with a bio-based oligomeric lactic acid (OLA) plasticizer at different concentrations between 15 wt% and 25 wt% in order to enhance PLA ductility and to get a fully biodegradable material with potential application in films manufacturing. OLA was an efficient plasticizer for PLA, as it caused a significant decrease on glass transition temperature (Tg) while improving considerably ductile properties. Only one Tg value was observed in all cases and no apparent phase separation was detected. Films obtained by compression moulding were stored during 3 months under ambient controlled conditions and thermal, mechanical, structural and oxygen barrier properties were studied in order to evaluate the stability of the PLA–OLA films over time. Blends with 20 and 25 wt% OLA remained stable and compatible with PLA within the ageing period. Besides, PLA–20 wt% OLA formulation was the only one which maintained its amorphous state with adequate thermal, mechanical and oxygen barrier properties for flexible films manufacturing.

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Glucose dehydrogenase (EC 1.1.1.47) from the halophilic Archaeon Haloferax mediterranei belongs to the medium-chain alcohol dehydrogenase superfamily and requires a zinc ion for catalysis. The zinc ion is coordinated by a histidine, a water molecule and two other ligands from the protein or the substrate, which vary during the catalytic cycle of the enzyme. In many enzymes of this superfamily one of the zinc ligands is commonly cysteine, which is replaced by an aspartate residue at position 38 in the halophilic enzyme. This change has been only observed in glucose dehydrogenases from extremely halophilic microorganisms belonging to the Archaea Domain. This paper describes biochemical studies and structural comparisons to analyze the role of sequence differences between thermophilic and halophilic glucose dehydrogenases which contain a zinc ion within the protein surrounded by three ligands. Whilst the catalytic activity of the D38C GlcDH mutant is reduced, its thermal stability is enhanced, consistent with the greater structural similarity between this mutant and the homologous thermophilic enzyme from Thermoplasma acidophilum.

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The preparation of imidazolium and benzimidazolium salts with hydroxyl or carboxylate functions has been achieved using straightforward synthetic pathways. These salts in combination with palladium(II) acetate give active catalytic systems for Suzuki reaction. A comparative study has been performed, which has revealed that both the heterocycle and the functional group are important for the catalytic activity and stability of the catalyst.