Retargeting of heterologous enzymes results in improved β-carotene synthesis in Saccharomyces cerevisiae.

Aims: Carotenoids are a class of hydrophobic substances that are important as food and feed colorants and as antioxidants. The pathway for β-carotene synthesis has been expressed in various yeast species, albeit with rather low yields and titers. The inefficient conversion of phytoene to lycopene is often regarded as a bottleneck in the pathway.

Exact symmetries in the velocity fluctuations of a hot Brownian swimmer.

Symmetries constrain dynamics. We test this fundamental physical principle, experimentally and by molecular dynamics simulations, for a hot Janus swimmer operating far from thermal equilibrium. Our results establish scalar and vectorial steady-state fluctuation theorems and a thermodynamic uncertainty relation that link the fluctuating particle current to its entropy production at an effective temperature.

Enhanced fed-batch fermentation of 2,3-butanediol by Paenibacillus polymyxa DSM 365.

Fed-batch fermentations for the production of 2,3-butanediol (BDL) with Paenibacillus polymyxa DSM 365 were investigated in 2-L-fermenters. A suitable micro-aerobic set-up enabled high product selectivity of up to 98% R,R-BDL towards meso-BDL and acetoin. Up to 111 g L(-1)R,R-BDL within 54 h could be achieved with sufficient supply of complex medium (yeast extract).

Continuous asymmetric ketone reduction processes with recombinant Escherichia coli.

The reduction of methyl acetoacetate was carried out in continuously operated biotransformation processes catalyzed by recombinant Escherichia coli cells expressing an alcohol dehydrogenase from Lactobacillus brevis. Three different cell types were applied as biocatalysts in three different cofactor regeneration approaches. Both processes with enzyme-coupled cofactor regeneration catalyzed by formate dehydrogenase or glucose dehydrogenase are characterized by a rapid deactivation of the biocatalyst.

Isolation and characterisation of a novel stress-inducible PDI-family gene from Aspergillus niger.

Current strategies to improve the secretion of heterologous proteins in Aspergillus niger include the manipulation of chaperones and foldases specific to the endoplasmic reticulum (ER). A family of ER-specific proteins which share active-site homology wit protein disulfide isomerase (PDI) has been identified from other systems, many of which are inducible by agents which cause malfolding of proteins in the ER. Here we report identification of tigA from Aspergillus niger and erp38 from Neurospora crassa, two novel members of the PDI superfamily of proteins.