Journal
CHEMISTRYSELECT
Volume 7, Issue 48, Pages -Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/slct.202203883
Keywords
Selenoesters; enzymatic kinetic resolution; lipases; alcohols; diselenides
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Funding
- National Council for Scientific and Technological Development (CNPq, Brazil) [Proc. 456834/2014]
- Coordination for the Improvement of Higher Level Personnel (CAPES, Brazil)
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This study demonstrates the use of selenoesters as acyl donors in lipase-catalyzed enzymatic kinetic resolution of chiral alcohols. The results show that lipases can effectively cleave the C-Se bond of selenoesters, leading to the successful synthesis of enantiopure compounds. The enzymatic reaction is accelerated in an oxygen atmosphere, and the purification process is simple and easy.
Lipase-catalyzed enantioselective synthetic reactions employing enol esters, activated esters, anhydrides, and oximes as acyl donors is a well-consolidated strategy towards enantiopure compounds. However, lipases can also cleave the C-S bond of thioesters, proving that other classes of substances can be used as acyl donors in lipase-catalyzed transformations. Herein we describe the application of selenoesters as a new class of acyl donors in enzymatic kinetic resolution of chiral alcohols. A series of selenoesters was successfully employed in the resolution of chiral primary and secondary alcohols, demonstrating that lipases can also cleave the C-Se bond. Assays using selenoesters as acyl donors in lipase-catalyzed reactions furnished enantiopure compounds (e.e.>99 %) and enantiomeric ratio (E>200). We also observed that the enzymatic reaction is accelerated in an oxygen atmosphere and performing a preparative scale reaction could demonstrate how simple and easy the purification process is to recover the diselenide formed during the resolution.
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