BACKGROUND Lipases including the lipase from Burkholderia cepacia are in a main focus in biotechnology research since many years because of their manifold possibilities for application in industrial processes. The application of Burkholderia cepacia lipase for these processes appears complicated because of the need for support by a chaperone, the lipase specific foldase. Purification and recons...

BACKGROUND 21-deoxycortisol (21-DF) is the key intermediate to manufacture pharmaceutical glucocorticoids. Recently, a Japan patent has realized 21-DF production via biotransformation of 17-hydroxyprogesterone (17-OHP) by purified steroid 11β-hydroxylase CYP11B1. Due to the less costs on enzyme isolation, purification and stabilization as well as cofactors supply, whole-cell should be preferent...

β-Peptides and their derivates are usually stable to proteolysis and have an increased half-life compared with α-peptides. Recently, β-aminopeptidases were described as a new enzyme class that enabled the enzymatic degradation and formation of β-peptides. As an alternative to the existing chemical synthesis routes, the aim of the present work was to develop a whole-cell biocatalyst for the synt...

Enantioselective production of (S)-2-phenyl-1-propanol is important as in order to be applied industry, a high degree optical purity required. Besides organocatalysts and metal complexes, biocatalysts can used for its synthesis their isolated form or whole-cell biocatalysts, both which have various advantages disadvantages. In this research, Saccharomyces cerevisiae, biocatalyst, recombinant ho...

BACKGROUND The bacterium Acetobacter sp. CCTCC M209061 is a promising whole-cell biocatalyst with exclusive anti-Prelog stereoselectivity for the reduction of prochiral ketones that can be used to make valuable chiral alcohols such as (R)-4-(trimethylsilyl)-3-butyn-2-ol. Although it has promising catalytic properties, its stability and reusability are relatively poor compared to other biocataly...

Highly selective enzymatic reductions of aldehydes to the corresponding alcohols was performed using an E. coli JM109 whole cell biocatalyst. A selective enzymatic method for the reduction of aldehydes could provide an eco-compatible alternative to chemical methods. The simplicity, fairly wide scope and the very high observed chemoselectivity of this approach are its most unique features.

Recombinant Escherichia coli systems expressing organophosphorous hydrolase (OPH) have been proposed for biotransformation of toxic organophosphate compounds. However, whole cell biocatalyst systems are critically disadvantaged due to substrate diffusion limitations. To enhance whole cell biocatalytic efficiency, we engineered E. coli, for the first time, to secrete metal ion cofactor-requiring...