Staphylococcus haemolyticus L62 (SHL62) lipase was displayed on the outer membrane of Escherichia coli using the OmpA signal peptide and the autotransporter EstA beta 8 protein. Localization of SHL62 lipase on the outer membrane of E. coli was confirmed using immunofluorescence microscopy and flow cytometry analysis. Lipase activity of the displayed SHL62 lipase was also measured using spectrophotometry and pH titration. SHL62 lipase activity of whole cells reached 2.0 U/ml culture (OD600 nm of 10) when it was measured by the p-nitrophenyl caprylate assay after being induced with 1 mM IPTG for 24 h. The optimum temperature and pH for the lipase was 45 degrees C and 10, respectively. Furthermore, it maintained more than 90% of maximum lipase activity at up to 50 degrees C and in a pH range of 5-9. The hydrolytic activity assay conduted with various substrates confirmed that p-nitrophenyl caprylate and corn oil were preferred substrates among various synthetic and natural substrates, respectively. The displayed SHL62 lipase produced fatty acid esters from various alcohols and plant oils through transesterification. (C) 2014 Elsevier Inc. All rights reserved.