Effect of the presence of surfactant and ionic liquids on the esterification of oleic acid catalyzed by immobilized lipase

Ionic liquids (ILs) and surfactants are widely used in order to increase the catalytic efficiency of lipases. In this sense, the present study aimed to evaluate the potential of different ionic liquids (C4MIM.Ac, C4MIM.HSO4, C4MIM.TF2N, C4MIM.BF4, C12MIM.I, and C12MIM.Cl), Aliquat 336 and di-2-ethylhexyl sodium sulfosuccinate (AOT) as adjuvants in the esterification of oleic acid with different alcohols catalyzed by Novozyme 435. First of all, it evaluates the effect of alkyl chain length of the alcohol and the positioning of the hydroxyl group. The selection of additives, made with isopropyl alcohol, pointed AOT and C4MIM.Ac as adjuvants effective on the potential of esterification of the enzyme (an increase of 35% in the potential of esterification). Using methanol, ethanol and 3-methyl-1-butanol, the C4MIM.Ac was proven not to be efficient, while the AOT shows adjuvant effect in the esterification of oleic acid with methanol (increasing in catalytic efficiency of enzyme in 21%).Key words: Esterification, di-2-ethylhexyl sodium sulfosuccinate (AOT), Ionic Liquids, Novozyme 435

The Enterovirus 71 A-particle Forms a Gateway to Allow Genome Release: A CryoEM Study of Picornavirus Uncoating

Since its discovery in 1969, enterovirus 71 (EV71) has emerged as a serious worldwide health threat. This human pathogen of the picornavirus family causes hand, foot, and mouth disease, and also has the capacity to invade the central nervous system to cause severe disease and death. Upon binding to a host receptor on the cell surface, the virus begins a two-step uncoating process, first forming an expanded, altered "A-particle", which is primed for genome release. In a second step after endocytosis, an unknown trigger leads to RNA expulsion, generating an intact, empty capsid. Cryo-electron microscopy reconstructions of these two capsid states provide insight into the mechanics of genome release. The EV71 A-particle capsid interacts with the genome near the icosahedral two-fold axis of symmetry, which opens to the external environment via a channel ~10 Å in diameter that is lined with patches of negatively charged residues. After the EV71 genome has been released, the two-fold channel shrinks, though the overall capsid dimensions are conserved. These structural characteristics identify the two-fold channel as the site where a gateway forms and regulates the process of genome release. © 2013 Shingler et al

Insights into Minor Group Rhinovirus Uncoating: The X-ray Structure of the HRV2 Empty Capsid

Upon attachment to their respective receptor, human rhinoviruses (HRVs) are internalized into the host cell via different pathways but undergo similar structural changes. This ultimately results in the delivery of the viral RNA into the cytoplasm for replication. To improve our understanding of the conformational modifications associated with the release of the viral genome, we have determined the X-ray structure at 3.0 Å resolution of the end-stage of HRV2 uncoating, the empty capsid. The structure shows important conformational changes in the capsid protomer. In particular, a hinge movement around the hydrophobic pocket of VP1 allows a coordinated shift of VP2 and VP3. This overall displacement forces a reorganization of the inter-protomer interfaces, resulting in a particle expansion and in the opening of new channels in the capsid core. These new breaches in the capsid, opening one at the base of the canyon and the second at the particle two-fold axes, might act as gates for the externalization of the VP1 N-terminus and the extrusion of the viral RNA, respectively. The structural comparison between native and empty HRV2 particles unveils a number of pH-sensitive amino acid residues, conserved in rhinoviruses, which participate in the structural rearrangements involved in the uncoating process

Bioepoxidation of isosafrol catalyzed by radish and turnip peroxidases

Peroxidases (PODs) from radish (Raphanus sativus L.) and turnip (Brassica napus L.) were extracted and precipitated with ammonium sulfate using a simple, low cost and quick method. The activities of all steps performed by the vegetable PODs were measured via guaiacol assay. The epoxidation of isosafrol, catalyzed by radish (R. sativus L.) and turnip (B. napus L.) peroxidases was conducted in 20% (v/v) aqueous ethanol solution using 30% (v/v) H2O2 as the terminal oxidant. High conversion (88%) and selectivity (>98%) were obtained after 48 h. The products of the reaction were analyzed by high resolution gas chromatography (GC) and mass spectrometry. Key words: Raphanus sativus L, Brassica napus L., peroxidase, epoxidation, isosafrol. Abbreviation: HRP, Horseradish peroxidase; GC, gas chromatography; POD, peroxidase

Cocaine conditioned place preference: unexpected suppression of preference due to testing combined with strong conditioning

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