Immobilization of lipase on bamboo charcoal was confirmed by spectra of FTIR, UV-Vis, and XPS. Under optimal conditions, the immobilized lipase retains 87% of the hydrolytic activity of the free lipase. Structural changes of the immobilized lipase were analyzed by circular dichroism and FTIR spectra, indicating that the secondary structure of the lipase was preserved well after immobilization. For catalyzing the enantioselective reaction in heptane, the catalysis efficiency of the immobilized lipase is 1.4 times that of free lipase. Immobilized lipase maintains the selectivity of free lipase.