Efforts have recently been made toward the study of interactions of phospholipid with various enzymes. It seems that phospholipids may be directly involved in regulating the enzyme activity. In this work, three phospholipid analogous polymers (PAPs), containing hydrophobic octyloxy, dodecyloxy, and octadecyloxy groups (abbreviated as 8-PAP, 12-PAP, and 18-PAP, respectively), were tethered on polypropylene hollow fiber microfiltration membrane (PPHFMM) to create a biocompatible interface for lipase immobilization. Lipase from Candida rugosa was immobilized on these PPHFMMs by adsorption. The adsorption capacity, activity, and thermal stability of enzyme on the PAP-modified PPHFMMs were compared with those of enzyme on the nascent ones. It was found that, as for the PAP-modified PPHFMMs, the adsorption capacities of lipase are lower than that of the nascent ones, while the activity retention of immobilized lipase increases from 57.5% to 74.1%, 77.5%, and 83.2% respectively for the 8-PAP-, 12-PAP-, and 18-PAP-modified PPHFMMs. In addition, the experimental results of thermal stability show that the residual activity of the immobilized lipase at 50 degreesC for 2 h is 62% for the 8-PAP-modified PPHFMM, 59% for the 12-PAP-modified PPHFMM, and 66% for the 18-PAP-modified PPHFMM, which are also higher than that of the nascent ones.