Preparation of Aligned Ultra-long and Diameter-controlled Silicon Oxide Nanotubes by Plasma Enhanced Chemical Vapor Deposition Using Electrospun PVP Nanofiber Template

Well-aligned and suspended polyvinyl pyrrolidone (PVP) nanofibers with 8 mm in length were obtained by electrospinning. Using the aligned suspended PVP nanofibers array as template, aligned ultra-long silicon oxide (SiOx) nanotubes with very high aspect ratios have been prepared by plasma-enhanced chemical vapor deposition (PECVD) process. The inner diameter (20–200 nm) and wall thickness (12–90 nm) of tubes were controlled, respectively, by baking the electrospun nanofibers and by coating time without sacrificing the orientation degree and the length of arrays. The micro-PL spectrum of SiOx nanotubes shows a strong blue–green emission with a peak at about 514 nm accompanied by two shoulders around 415 and 624 nm. The blue–green emission is caused by the defects in the nanotubes

Conversion of alcohols to enantiopure amines through dual-enzyme hydrogen-borrowing cascades.

α-Chiral amines are key intermediates for the synthesis of a plethora of chemical compounds at industrial scale. We present a biocatalytic hydrogen-borrowing amination of primary and secondary alcohols that allows for the efficient and environmentally benign production of enantiopure amines. The method relies on a combination of two enzymes: an alcohol dehydrogenase (from Aromatoleum sp., Lactobacillus sp., or Bacillus sp.) operating in tandem with an amine dehydrogenase (engineered from Bacillus sp.) to aminate a structurally diverse range of aromatic and aliphatic alcohols, yielding up to 96% conversion and 99% enantiomeric excess. Primary alcohols were aminated with high conversion (up to 99%). This redox self-sufficient cascade possesses high atom efficiency, sourcing nitrogen from ammonium and generating water as the sole by-product

Generation of amine dehydrogenases with increased catalytic performance and substrate scope from ε-deaminating <i>L</i>-Lysine dehydrogenase

Amine dehydrogenases (AmDHs) catalyse the conversion of ketones into enantiomerically pure amines at the sole expense of ammonia and hydride source. Guided by structural information from computational models, we create AmDHs that can convert pharmaceutically relevant aromatic ketones with conversions up to quantitative and perfect chemical and optical purities. These AmDHs are created from an unconventional enzyme scaffold that apparently does not operate any asymmetric transformation in its natural reaction. Additionally, the best variant (LE-AmDH-v1) displays a unique substrate-dependent switch of enantioselectivity, affording S- or R-configured amine products with up to >99.9% enantiomeric excess. These findings are explained by in silico studies. LE-AmDH-v1 is highly thermostable (Tm of 69 °C), retains almost entirely its catalytic activity upon incubation up to 50 °C for several days, and operates preferentially at 50 °C and pH 9.0. This study also demonstrates that product inhibition can be a critical factor in AmDH-catalysed reductive amination