Stereoselective hydrolysis of (±)-2-(4-hydroxyphenyl)propionic acid ethyl ester (2-HPPAEE) by lipase catalyzed in aqueous system was investigated. Lipase AK with higher catalytic activity and enantioselectivity was selected as catalyst. Simultaneously, factors affecting the conversion of substrate (c) and the enantiomeric excess of product (eep) were optimized. The optimal conditions were established, involving 45 °C of temperature, 5.5 of pH, 10 mg of lipase AK dosage, 0.04 mmol of substrate dosage and 40 h of reaction time. Under the optimum conditions, c and eep could reach up to 49% and 98%, respectively.