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A new biocatalytic route to enantiopure N-carbamoyl amino acids by fast enzyme screening |
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| Authors: | Harald Trauthwein Oliver MayUwe Dingerdissen Stefan BuchholzKarlheinz Drauz |
| Institution: | a Degussa AG, Project House Catalysis, Industriepark Hoechst G830, D-65926 Frankfurt a. M., Germany b Degussa AG, Project House Biotechnology, Rodenbacher Chaussee 4, D-63457 Hanau-Wolfgang, Germany c Degussa AG, Business Unit Fine Chemicals, D-63457 Hanau-Wolfgang, Germany |
| Abstract: | The enantioselective enzymatic deamidation of (rac)-N-carbamoyl amino acid amides (Cbm-AA-NH2) to enantiopure (L)-N-carbamoyl amino acids (Cbm-AA-OH) is described for the first time. Via fast screening methods of biocatalysts several proteases like Chirazyme P1, Chirazyme P2 and Subtilisin were identified, which give conversions of up to 47% and >98% ee. This conversion is most productive on aliphatic and primary amino acids. |
| Keywords: | biocatalysis N-carbamoyl amino acid amide proteases enantioselective enzymatic deamidation HTS |
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