208180-85-2Relevant academic research and scientific papers
Enzymes in organic chemistry VI [1]. Enantioselective hydrolysis of 1-chloroacetoxycycloalkylmethylphosphonates with lipase AP 6 from Aspergillus niger and chemoenzymatic synthesis of chiral, nonracemic 1-aminocyclohexyl-methylphosphonic acids
Wuggenig, Frank,Hammerschmidt, Friedrich
, p. 423 - 436 (2007/10/03)
Racemic α-chloroacetoxyphosphonates derived from cycloalkanecarbaldehydes and three branched aldehydes were prepared and tested for kinetic resolution by lipase AP 6 which hydrolyses preferentially the (S) esters. The enantiomeric excess and the reaction rate are significantly influenced by the size of the cycloalkyl group. The optical antipodes of α-hydroxycyclohexylmethylphosphonates (3d; ee 90% and ≥ 99%, respectively) were transformed into the corresponding α-aminophosphonic acids 6.
Enzymes in organic chemistry, 8.[1] Protease-catalyzed kinetic resolution of α-chloroacetoxyphosphonates in a biphasic system
Hammerschmidt, Friedrich,Wuggenig, Frank
, p. 231 - 238 (2007/10/03)
Protease Chirazyme P-2 hydrolyses racemic α-chloroacetoxyphosphonates (±)-1 enantioselectively to furnish α-hydroxyphosphonates (R)-(-)-2 with ee's ranging from 31 to 97% at a conversion of 45% and unreacted esters (S)-(+)-1.
