Alcohol dehydrogenase and its use for the enzymatic production of chiral hydroxy compounds
AssigneeForschungszentrum Julich GmbH
InventorsWerner Hummel, Bettina Riebel
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Abstract
Stable microbial enzyme with alcohol dehydrogenase activity having an activity maximum at ca. 50.degree. C., process for its isolation and its use for the enantioselective reduction/oxidation of organic keto compounds/hydroxy compounds wherein, depending on the type of the starting compounds R- or S-hydroxy compounds are obtained. In particular an alcohol dehydrogenase obtainable from Lactobacillus brevis has proven to be suitable.
Claims13
A purified microbial alcohol dehydrogenase which reacts with acetophenone to form R-phenylethanol, wherein said purified enzyme retains at least 95% activity after about 30 minutes incubation over a temperature range of about 20.degree. C. to about 60.degree. C.
A purified Lactobacillus alcohol dehydrogenase which reacts with acetophenone to form R-phenylethanol, wherein said purified enzyme retains at least 95% activity after about 30 minutes incubation over a temperature range of about 20.degree. C. to about 60.degree. C., wherein the N-terminus of said alcohol dehydrogenase has the amino acid sequence set forth in SEQ ID NO:
- 1, with the proviso that amino acid 1 is Ser, rather than Thr, amino acid 2 is Asn rather than Asp, amino acid 5 is Asp rather than Lys, amino acid 24 is Thr rather than Asp, and amino acid 34 is Met rather than Val.
A purified Lactobacillus alcohol dehydrogenase which reacts with acetophenone to form R-phenylethanol, wherein said purified enzyme retains at least 95% activity after about 30 minutes incubation over a temperature range of about 20.degree. C. to about 60.degree. C., wherein the N-terminal amino acid of said purified alcohol dehydrogenase is Ser, the second amino acid is Asn, the fifth amino acid is Asp, the twenty-fourth amino acid is Thr, and the thirty fourth amino acid is Met.
Dependencies are inferred from the claim text.