Asymmetric transesterification resolution of para⁃( R, S )⁃α⁃phenylethanol was conducted by lipase YCJ01. The resolution conditions of para⁃(R,S)⁃α⁃phenylethanol were optimized. Reaction was carried out in isopropyl ether using vinyl acetate as acyl donors with 5 g/L lipase YCJ01 and 180 mmol/L 1⁃(4⁃methylphenyl)ethanol. The mixture was incubated at 50℃ for 21 h. After the reaction,the substrate conversion could reach 49�96% with e�e.s=97�1%,e�e.p=97�2%,E>200�Similarly,high enantiomeric purity(e�e.s=97�7%,e�e.p=98�4%,E>200) and substrate conversion(49�82%) were achieved at 30℃ after 12 h in isopropyl ether with 2�5 g/L lipase YCJ01 and 150 mmol/L 1⁃( 4⁃methoxyphenyl ) ethanol, vinyl butyrate as acyl donors. All results illustrated that lipase YCJ01 was an exploitable biocatalyst for chiral resolution of pharamaceutical intermediate.%利用脂肪酶YCJ01催化拆分对位取代α苯乙醇衍生物。以异丙醚为反应介质，采用乙酸乙烯酯作为酰基供体，对180 mmol／L的1（4甲基苯基）乙醇进行选择性酯化，脂肪酶粗酶粉添加量为5 g／L，50℃反应21 h后，底物转化率可达49�96％，对映体过量值e�e． s、e�e． p值分别为97�1％和97�2％，对映体选择性E＞200；同样，对1（4甲氧基苯基）乙醇进行选择性酯化，酰基供体为丁酸乙烯酯，底物浓度150 mmol／L，脂肪酶粗酶粉添加量为2�5 g／L，30℃反应12 h后，底物转化率为49�8％，e�e． s、e�e． p值分别为97�7％和98�4％，对映体选择性E＞200，显示了很好的手性拆分效果。
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