Relatively poor heterologous protein yields have limited the commerical applications of Galactomyces geotrichum lipase I (GGI I) efficacy trials. To address this, we have redesigned the GGI I gene to preferentially match codon frequencies of Pichia pastoris (P. pastoris) while retaining the same amino acid sequence. The wild type and codon optimised GGI I (GGI I-wt and GGI I-op) were synthesised and cloned into pPICZ alpha A with an N-terminal 6 x His tag sequence and expressed in P. pastoris X 33. The hydrolytic activity of GGI I-op was 150 U/mL, whereas the activity of the GGI I-wt could not be detected. GGI I-op recombinant proteins were purified by Ni-affinity chromatography and then characterised. The identity and purity of GGI I were confirmed by SDS-PAGE, MALDI-TOF mass spectrometry and Western blot analysis. Enzymatic deglycosylation was used to show that the lipase is a glycosylated protein, containing similar to 10% sugar. The molecular weight (MW) of the GGI I secreted by recombinant P. pastoris was approximated at 63 kDa. The optimum pH and temperature of the recombinant lipase were 8.0 and 35 degrees C, respectively. The enzyme was active over a broad pH range (7.0-9.0) and temperature range (20 degrees C similar to 45 degrees C). The lipase showed high activity toward medium- and long-chain fatty acid methyl esters (C8-C16) and retained much of its activity in the presence of Tween-80 and Trition X-100. Lipase activity was stimulated by Mg2+, Ca2+, Mn2+ and Cu2+ and inhibited by Fe2+, Fe3+, Zn2+ and Co2+. This lipase may prove useful to the detergent industry and in organic synthesis reactions. (C) 2017 Published by Elsevier Inc.