Development of an Immobilized Ketoreductase for Enzymatic (R)-1-(3,5-Bis(trifluoromethyl)phenyl)ethanol Production

Organic Process Research and Development

Volumn 19, Issue 7, 2015, Pages 695-700

  Li, Hongmei ^a   Moncecchi, Johannah ^a   Truppo, Matthew D ^a  

^a MERCK RESEARCH LABORATORIES   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ETHANOL;

BATCH MODES; CHIRAL ALCOHOLS; CHIRAL INTERMEDIATES; COVALENT BINDING; ETHANOL PRODUCTION; FLOW REACTORS; TRIFLUOROMETHYL; WATER SOLVENT SYSTEM;

ORGANIC SOLVENTS;

EID: 84937139834     PISSN: 10836160     EISSN: 1520586X     Source Type: Journal    
DOI: 10.1021/op5003215     Document Type: Article

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30. The remaining activity of 94% for the immobilized enzyme (stability study) was determined from the conversion in ketone reduction with the immobilized enzyme after it was packed for 7 days at 40 °C in the PFR versus the conversion with the immobilized enzyme packed fresh in the PFR under the same reaction conditions and residence time.
31. In Table 1, the ee values of the alcohol products with immobilized P1B2 are the same as or similar to those with the lyo enzyme P1B2 reaction system. The ee values in entries 6 and 7 could be lower or higher depending on the enzyme loading for both the immobilized and lyo enzyme systems.