Lipase YILip11 from Yarrowia lipolytica was expressed with a signal peptide encoding sequence in Arxula adeninivorans, Saccharomyces cerevisiae and Hansenula polymorpha using the Xplor (R) 2 transformation/ expression platform and an expression module with the constitutive Ancula-derived TEF1 promoter. The YlLip11 signal peptide was functional in all of the yeast hosts with 97% of the recombinant enzyme being secreted into the culture medium. However, recombinant YILipl 1 with His Tag fused at C-terminal was not active. The best recombinant YILipl 1 producing A. adeninivorans G1212/YRC102-YILipll transformant cultivated in shake flasks produced 2654 U/L lipase, followed by S. cerevisiae SEY6210/YRC103-YILip11 (1632 U/L) and H. polymorpha RB11/YRC103-YlLip11 (1144 U/L). Although the biochemical parameters of YILipl 1 synthesized in different hosts were similar, their glycosylation level and thermo stability differed. The protein synthesized by the H. polymorpha transformant had the highest degree of glycosylation and with a to of 60 min at 70 degrees C, exhibited the highest thermostability. (C) 2015 Elsevier Inc. All rights reserved.