Abstract: The enzyme activity of Candida antarctica lipase B (CALB) displaying Pichia pastoris was investigated.Results showed that the enzyme displays the highest activity at 50~60 ℃.Effect of separate substrates catalyzing by CALB was compared.In a case using 1,2-O-isopropylidene-α-D-glucofuranose (IpGlc) as the acyl receptor and myristic acid as the acyl donor,the effect of the polarity of organic solvent,the dosage of catalyst,the molar ratio of the substrates,the dosage of 4A molecular sieve,and initial water activity was studied.The suitable reaction conditions are as follows:acetone,5 mL;CALB (dry powder),0.3 g;n(IpGlc)∶n(myristic acid)=1∶3 (with IpGlc 0.5 mmol);no 4A molecular sieve to be used;water activity,a_w=0.11;reaction temperature,50 ℃;agitator speed,200 r/min for 72 h.The final yield achieves 91.25%.IpGlc-C14 reaction results of using CALB and Novozym 435 were compared and showed that Novozym 435 displays higher reaction rate,and CALB displays higher final yield.

Key words: sugar ester, surface displaying technology, lipase B whole-cell biocatalyst, 1,2-O-isopropylidene-α-D-glucofuranose