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Bachelor or Master Thesis: Investigation of imine reductases in micro-aqueous system

Advertising institute: IBG-1 - Biotechnology
Reference number: D096/2014, Chemistry, biochemistry, biotechnology

Background
Over the last decades the industrial application of enzymes is increasing due to the high selectivities achievable, typically under mild reaction conditions. In our group 3 enzyme toolboxes (oxidoreductases, tranferases and lyases) were established. Each toolbox contains a collection of enzymes catalyzing the same kind of reaction but having different substrate specificity and stereoselectivity. The scope of our research is the synthesis of industrially relevant molecules and building blocks by combining chemo-enzymatic catalytic steps. Both isolated enzymes and whole cells are used taking in consideration the corresponding advantages and disadvantages related to each type of catalyst. The possibility of performing reactions in non-conventional media (e.g. organic solvents, micro-aqueous system) is as well explored in order to increase substrate concentration and facilitate the downstream process.

Project description
Chiral amines represent a class of molecules particularly important in the industrial field as building blocks for biologically active pharmaceutical compounds. Several catalytic methods have been developed mostly involving transition-metal and organocatalysts. Within the field of biocatalysis classes of enzymes such as transaminases and monoamine oxidases have been used and many successful results can be found in literature. Imine reductases catalyze the reduction of imines to amines by using NADPH as a cofactor. So far this class of enzymes has not intensively studied and most of the literature dates back only to the last decade. The goal of the project is the investigation of some imine reductases in micro-aqueous system by using as substrates cyclic and acyclic imines. For the successful cases the following optimization will be done and the possibility to implement the reaction in an existing cascade reaction explored.

Please send your application together with your CV and marks to:
Zaira Maugeri
Biocatalysis & Biosensors
IBG-1: Biotechnology
Forschungszentrum Jülich GmbH
52425 Jülich
Tel: +49 2461 61-5199
E-Mail: z.maugeri@fz-juelich.de


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