The properties of Candida antarctica lipase B (CAL-B) displayed on yeast cell surface were studied in this paper . Catalytic activity of displayed CAL-B was measured in the hydrolysis of p-nitrophenyl esters with various acyl chain lengths. The results showed that the optimal conditions of enzymatic hydrolysis were as follows: pH value of 8.0~8.5 and temperature of 40~45 ℃. Displayed CALB was stable at pH 7.5~8.0 and remained 88% of activity after incubation at 40 ℃ for 4 h. Besides，the whole-cell biocatalyst showed high substrate specificity with p-nitrophenyl butyrate being of the most suitable substrate. It was also found that the lipase activity of the yeasts was enhanced by Ca2+ and Mg2+, but inhibited by Co2+ and Cu2+.