Nurhasanah_2017_J.Pure.Appl.Microbiol_11_135

Three lipase genes namely LK2, LK3 and LK5 were successfully sub-cloned into expression vector pET30a. The recombinant vectors were heterologically expressed into Escherichia coli BL21 (DE3) by 1 mM IPTG induced at 37C. The protein with the size of 32, 31 and 28 kDa with correspond to LK2, LK3 and LK5 clones were over expressed following SDS-PAGE analysis. Further analysis to quantity the level of expression showed that the protein were over expressed at around 30, 44 and 21% of the total protein for LK2, LK3 and LK5 respectively. The lipolytic activity of the proteins by using lauric acid (C12) as substrate at 50C, appeared that LK2 showed the highest activity among the other (1.49U/mg) followed by LK5 (1,10U/mg) and the lowest activity is LK3 (0.94U/mg).