Kinetic resolution of (R,S)-1,2-isopropylidene glycerol (solketal) ester derivatives by lipases

AbstractA study on the enantioselective hydrolysis of (R,S)-1,2-isopropylidene glycerol (4-hydroxymethyl-2,2-dimethyl-1,3-dioxolane, solketal) octanoate catalyzed by different lipases was carried out. Among them, Pseudomonas sp. lipase proved to be the most effective. It was shown that the ester bearing the longer octanoyl acyl chain is a more suitable substrate for this lipase compared to the acetate counterpart. By properly combining enzyme load, temperature and reaction time, either the (S)-alcohol or the remaining ester could be obtained in moderate to high selectivities. Ethyl acetate was found to be the best solvent for the kinetic resolutions effected by such lipase but our results show that toluene may prove useful

Lipidomic profile as a non-invasive tool to predict endometrial receptivity in freeze-all cycles

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Early-branching gut fungi possess a large, comprehensive array of biomass-degrading enzymes

The fungal kingdom is the source of almost all industrial enzymes in use for lignocellulose bioprocessing. We developed a systems-level approach that integrates transcriptomic sequencing, proteomics, phenotype, and biochemical studies of relatively unexplored basal fungi. Anaerobic gut fungi isolated from herbivores produce a large array of biomass-degrading enzymes that synergistically degrade crude, untreated plant biomass and are competitive with optimized commercial preparations from Aspergillus and Trichoderma. Compared to these model platforms, gut fungal enzymes are unbiased in substrate preference due to a wealth of xylan-degrading enzymes. These enzymes are universally catabolite-repressed and are further regulated by a rich landscape of noncoding regulatory RNAs. Additionally, we identified several promising sequence-divergent enzyme candidates for lignocellulosic bioprocessing