Hydrolytic and Transesterification Activities of Thermostable Lipase ITB1.1

Abstract

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 o C 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 o C 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.

Novel thermostable lipase produced by a thermo-halophilic bacterium that catalyses hydrolytic and transesterification reactions

“…Lauric acid is indeed the primary fatty acid found in coconut oil, comprises nearly half of the total (Khrisna et al, 2010). The result of this study was relevant to the result of Brilliantoro (Brilliantoro et al, 2015), where methyl laurate is the main component of the transesterification product of coconut oil.…”

Cloning, heterologous expression, and characterization of a novel thioesterase from natural sample

“…Some thermostable lipases and esterases from thermophilic organisms were cloned and characterized, from various natural sources such as hot springs, craters or compost, both through cultivation [14,16,17,18,19,20,21,22] and metagenomics approaches [23]. In this report, cloning, heterologous expression, and characterization of a novel gene from natural sample of Domas Hot spring, West Java, namely TESITB was described.…”