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An efficient lipase-catalyzed enantioselective hydrolysis of bu-tyryloxyalkanephosphonates in water-equilibrated diisopropylether was developed. The relationship between the substrates’structure and the reactivity, as well as the enantioselectivity ofthis enzymatic transformation was studied. The catalytic pref-erence of crude Candida rugosa lipase toward such moleculeswas assigned according to modified Mosher’s method and X-ray crystallographic analysis. Optically pure 2-hydroxy-2-arylethanephosphonates, 3-hydroxy-3-phenylpropanephosphon-ate, and 3, 3, 3-trifluoro-2-hydroxypropanephosphonates wereconveniently prepared in this manner.
The efficient between the substrates and structure of the reactivity, as well as the enantioselectivity of the enzymatic transformation was studied. The catalytic pref-erence of crude Candida rugosa Lipase toward such molecules were assigned according to modified Mosher’s method and X-ray crystallographic analysis. Optically pure 2-hydroxy-2-arylethanephosphonates, 3-hydroxy- 3 -phenylpropanephosphon-ate, and 3, prepared in this manner.