| Autor: |
Pogorevc, Mateja, Strauss, Ulrike T., Hayn, Marianne, Faber, Kurt |
| Zdroj: |
Chemical Monthly / Monatshefte für Chemie; Jun2000, Vol. 131 Issue 6, p639-644, 6p |
| Abstrakt: |
Biocatalytic resolution of the tertiary terpene alcohol (±)-linalool was accomplished via hydrolysis of its corresponding acetate ester using two highly enantiospecific enzymes ( E > 100). The latter were identified in a crude cell-free extract of Rhodococcus ruber DSM 43338 and could be separated by (partial) protein purification. Since they showed opposite enantiopreference, they were termed ( R)- and ( S)-linalyl acetate hydrolase (LAH). The activity and selectivity of the enzyme preparations was markedly dependent on the fermentation conditions. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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