Publications by authors named "Eszter Kokai"

This study focuses on polyamide 6/organo-modified montmorillonite (PA6/OMMT) nanocomposites as potential liner materials, given the growing interest in enhancing the performance of type IV composite overwrapped hydrogen storage pressure vessels. The mechanical properties of PA6/OMMT composites with varying filler concentrations were investigated across a temperature range relevant to hydrogen storage conditions (-40 °C to +85 °C). Liner collapse, a critical issue caused by rapid gas discharge, was analyzed using an Ishikawa diagram to identify external and internal factors.

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The chemistry of the 5,7-dihydro-6-pyrrolo[2,3-]pyrimidin-6-one (1,3-diazaoxindole) compound family, possessing a drug-like scaffold, is unexplored. In this study, the alkylation reactions of (7)-unsubstituted 5-isopropyl-1,3-diazaoxindoles bearing various substituents at the (2) position have been investigated. The starting compounds were synthesized from the (5)-unsubstituted parent compounds by condensation with acetone and subsequent catalytic reduction of the 5-isopropylidene moiety.

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The paper provides a comprehensive review of the base-catalysed C3-alkylation of N-unprotected-3-monosubstituted oxindoles. Based on a few, non-systematic studies described in the literature using butyllithium as the deprotonating agent, an optimized method has now been elaborated, via the corresponding lithium salt, for the selective C3-alkylation of this family of compounds. The optimal excess of butyllithium and alkylating agent, and the role of the halogen atom in the latter (alkyl bromides vs.

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Phenylalanine ammonia-lyase (PAL), found in many organisms, catalyzes the deamination of l-phenylalanine (Phe) to (E)-cinnamate by the aid of its MIO prosthetic group. By using PAL immobilized on magnetic nanoparticles and fixed in a microfluidic reactor with an in-line UV detector, we demonstrated that PAL can catalyze ammonia elimination from the acyclic propargylglycine (PG) to yield (E)-pent-2-ene-4-ynoate. This highlights new opportunities to extend MIO enzymes towards acyclic substrates.

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