کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
4756605 | 1419013 | 2017 | 5 صفحه PDF | دانلود رایگان |
- A carbonyl reductase was discovered to reduce NBPO to (R)-NBHP with high activity.
- A GDH-catalyzed cofactor-recycling system was used to regenerate NADPH.
- The process was optimized and applied to produce (R)-NBHP (>Â 99% ee).
- The asymmetric reduction was conducted at high substrate loading (400Â g/L).
The 3-hydroxypiperidine moiety is a privileged scaffold encountered in many bioactive compounds. An NADPH-dependent reductase (YGL039W) from Kluyveromyces marxianus ATCC 748 was isolated to show excellent catalytic activity in (R)-N-Boc-3-hydroxypiperidine [(R)-NBHP] production. Using a GDH-catalyzed cofactor-recycling system to ensure a sufficient supply of NADPH, the effects of temperature, pH, metal ions, substrate concentration, biocatalyst dosage, and cofactors on the YGL039W-catalyzed bioreduction were investigated and optimized. Finally, an extremely high concentration of N-Boc-piperidin-3-one (NBPO, 400Â g/L) could be completely reduced to (R)-NBHP (>Â 99% ee), with a total turnover number of 20,000. This process shows significant potential for the industrial production of (R)-NBHP.
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Journal: Catalysis Communications - Volume 97, 5 July 2017, Pages 5-9