Lipase is one of the most important industrial enzymes applied widely in food, textile, papermaking and pharmaceutical industries. The alkaline lipase gene from Acinetobacter radioresistens CMC-1 was synthesized with its own signal peptide removed followed by codon optimization, and then cloned into the secreted expression vector pPICZαA. The constructed plasmid was named as pPICZαA-ARL. The recombinant plasmid was used to transform into the Pichia pastoris X33. One of the best transformants harboring ARL integrated into the P. pastoris genomic DNA was cultured in shake flask. The maximum activity of the culture supernatant was 65 U/mL. The properties of the recombinant lipase was partial characterized. The results showed that the recombinant lipase had an optimal activity at 50 ℃ and pH 9.0 and the optimum substrate of recombinant ARL was 4-nitrophenyl caprylate, which seemed a little difference from the wild one.