Hereby multi-enzymatic cascade reactions are developed for the synthesis of natural and unnatural carbohydrates. The highly valuable dihydroxyacetone phosphate is the key intermediate in these cascades. The thermodynamic control is based on the formation and hydrolysis of phosphorylated intermediates by acid phosphatase and the synthetic key step is the C-C bond formation by DHAP-dependent aldolases. Possibilities of and limitations on the use of alkaline phosphatase and transketolase are also investigated.
Another important part of this research is the implementation of such already established cascades with a more efficient process. This is based on the immobilization of the enzymes and their use in different types of packed-bed reactors. This allows to switch from one-pot batch methods to the labour-free technology of continuous flow systems for the synthesis of highly valuable compounds.
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