Lipase from Candida rugosa (CRL) and cholesterol esterase (CE) catalyzed the enantioselective hydrolysis of pendant acetates in chiral phosphines and phosphine oxides. The enantioselectivity for most substrates was modest (E = 1.5–4.8), but both hydrolases showed high enantioselectivity for one substrate, ArPhMeP═O (Ar =1-(2-acetoxy)naphthyl, 4c), E = 81 (CRL) and 32 (CE). Preparative-scale resolution of (±)-4c (1.0 g) catalyzed by CRL yielded enantiomerically-enriched starting acetate, (S)–(+)-4c, 0.48 g, 90% ee as well as product alcohol, (R)-(–)-4b (Ar = 1-(2-hydroxy)-naphthyl), 0.39 g, 88% ee. Recrystallization of 4b from toluene raised the enantiomeric purity to >95% ee. Standard chemical steps followed by stereospecific reduction gave both enantiomers of phosphine ArPhMeP (Ar = 1-(2-methoxy)naphthyl) with 96–97% ee. This phosphine is an analog of PAMP (Ar = 2-methoxyphenyl), a chiral phosphine used in asymmetric synthesis.