eng Oriental Scientific Publishing Company Biosciences Biotechnology Research Asia 0973-1245 2015-04-28 12 1 01 06 4287 article Ridho Brilliantoro 1 Robby Zidny 1 Made Puspasari Widhiastuty 1 Akhmaloka 1 Biochemistry Research Group, Faculty of Mathematics and Natural Sciences, Institut Teknologi Bandung, Jl. Ganesha 10, Bandung 40132, Indonesia. Heterologous expression of local thermostable lipase (Lipase ITB1.1) has been carried out by using pET-30a(+) vector in Escherichia coli BL21(DE3). SDS-PAGE analysis showed that the protein size is around 50 kDa. Hydrolytic activity was determined at 70 oC and pH 8 by using p-Nitrophenyl palmitate (pNPP) as substrate. The activity of partial purified enzyme was significantly increased (0.56 U/mg) compared to that the crude extract (0.25 U/mg). Lipase ITB 1.1 has highest specific activity (1.23 U/mg) at 85 oC and pH 9.5. Further, characterization of the enzyme suggested that the enzyme exhibited transesterification activity. GC-MS spectra of the reaction product indicated that the coconut oil (substrate) was converted into methyl esters. The results suggesting that Lipase ITB1.1 is potential enzyme for biodiesel production https://www.biotech-asia.org/vol12no1/hydrolytic-and-transesterification-activities-of-thermostable-lipase-itb1-1/ Thermostable enzyme; Lipase; Hydrolytic; Transesterification