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An innovative strategy for sustainable SO capture and conversion in novel imidazole-based deep eutectic solvents (DESs) is demonstrated in this work. These DESs exhibit an extremely high SO loading capacity (up to 1.39 g g) and excellent reversibility (15 recycles). The absorbed SO can be rapidly converted in situ to sulphur (up to 99% conversion) in the presence of HS at room temperature without any additives.

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The catalyst-free N-formylation of amines using CO as the C source and BHNH as the reductant has been developed for the first time. The corresponding formylated products of both primary and secondary amines are obtained in good to excellent yields (up to 96% of isolated yield) under mild conditions.

Under hydrothermal conditions and extremely high NaOH activity, ZnS forms nanostructures with complex morphologies that are based upon individual or interpenetrating nanosheets. Nanostructure morphology is independent of the size of the ZnS precursor (3 nm, 20 nm, or bulk) but varies systematically with NaOH concentration, producing compact microspheres, open nest- and flowerlike structures, and finally, individual nanosheets. The observations are consistent with a concept of nanostructure morphology controlled by a single parameterthe interfacial free energy of the ZnS (001) face. The synthesis of thermodynamically stable nanostructures open opportunities for new synthetic routes of materials with complex architectures.

In this study, laccase production was enhanced using mutant Shiraia sp. The Shiraia sp. GZS1 strain was mutated using ultraviolet irradiation, followed by screening of strains that were resistant to certain stressors. The mutant GZ11K2 was selected and used for further studies. 2,2′-Azino-bis(3-ethylben-zothiazoline-6-sulfonate) was used as substrate for both wild and mutant laccases at optimal pH (4.0). The mutant laccase exhibited a broader active pH range. The mutant laccase also showed a higher optimal catalytic temperature, more active under alkaline conditions, and higher temperature range than the wild one. The mutant strains produced higher yield of laccase than the wild strain even at high salinity of 3 g/L NaCl. Both laccases were mildly inhibited by sodium dodecyl sulfate (0.5 mM), ethanol (50%) and ethylenediaminetetraacetic acid (1 mM), and almost completely inhibited by NaN3 (20 μM) and DTT (1 mM), stable in the presence of metal ions except Ag + and Hg 2+. PRACTICAL APPLICATIONSLaccase is extensively used in various applications, such as pulp delignification, decoloration, biopolymer modification, biotransformation and food dechlorination. A newly isolated laccase-producing strain Shiraia sp. GZS1 and a genetically stable mutant GZ11K2 were established with 1.82 times laccase activity compared with that of the wild strain. The mutant Shiraia sp. GZ11K2 laccase was active over a wider pH and temperature ranges and more stable than the wild strain under neutral and alkaline conditions. The laccase from the mutant GZ11K2 with higher laccase productivity and enhanced enzyme properties can be used in biotechnological and industrial applications.