A refined picture of the native amine dehydrogenase family revealed by extensive biodiversity screening.

Native amine dehydrogenases offer sustainable access to chiral amines, so the search for scaffolds capable of converting more diverse carbonyl compounds is required to reach the full potential of this alternative to conventional synthetic reductive aminations. Here we report a multidisciplinary strategy combining bioinformatics, chemoinformatics and biocatalysis to extensively screen billions of sequences in silico and to efficiently find native amine dehydrogenases features using computational approaches. In this way, we achieve a comprehensive overview of the initial native amine dehydrogenase family, extending it from 2,011 to 17,959 sequences, and identify native amine dehydrogenases with non-reported substrate spectra, including hindered carbonyls and ethyl ketones, and accepting methylamine and cyclopropylamine as amine donor.

Purification and Characterization of Nit , a Robust Thermostable Nitrilase From .

Despite the success of some nitrilases in industrial applications, there is a constant demand to broaden the catalog of these hydrolases, especially robust ones with high operational stability. By using the criteria of thermoresistance to screen a collection of candidate enzymes heterologously expressed in , the enzyme Nit from the mesophilic organism was selected and further characterized. Its quick and efficient purification by heat treatment is of major interest for large-scale applications.

Nitrilase immobilization and transposition from a micro-scale batch to a continuous process increase the nicotinic acid productivity.

In recent years, many biocatalytic processes have been developed for the production of chemicals and pharmaceuticals. In this context, enzyme immobilization methods have attracted attention for their advantages, such as continuous production and increased stability. Here, enzyme immobilization methods and a collection of nitrilases from biodiversity for the conversion of 3-cyanopyridine to nicotinic acid were screened.

Complete Genome Sequences of Two Species Isolated from Marine Environments of the Pacific Ocean.

YsY11 and T9AD were both isolated from marine environments of the Pacific Ocean. Here, we report the whole-genome sequences of these two organisms. YsY11 consists of a single 4.

XszenFHal, a novel tryptophan 5-halogenase from Xenorhabdus szentirmaii.

Flavin-dependent halogenases (FHals) catalyse the halogenation of electron-rich substrates, mainly aromatics. Halogenated compounds have many applications, as pharmaceutical, agrochemicals or as starting materials for the synthesis of complex molecules. By exploring the sequenced bacterial diversity, we discovered and characterized XszenFHal, a novel FHal from Xenorhabdus szentirmaii, a symbiotic bacterium of entomopathogenic nematode.