Characterization of two novel thermostable esterases from Thermoanaerobacterium thermosaccharolyticum

This paper first describes characterization of two thermostable esterases (ThLip1 and ThLip2) from the thermophilic bacterium Thermoanaerobacterium thermosaccharolyticum DSM 571. The recombinant esterase ThLip1 was active at 80 °C, pH 6.5 and maintained approx. 85% of original activity after 2 h incubation at 75 °C. Kinetic parameters, Km, Vmax and kcat/Km for 4-Nitrophenyl caprylate (pNPC) were 3.52 ± 0.47 mM, 191.18 ± 1.82 μmol min−1 mg−1 and 20.80 ± 0.07 mM−1 s−1, respectively. The purified recombinant esterase ThLip2 was optimally active at pH 6.5 and 75 °C and it was stable against a pH range of 6.0–8.0 possessing 2 h half-life at 80 °C. Kinetic experiments at 75 °C with pNPC as a substrate gave a Km of 3.37 mM, Vmax of 578.14 μmol min−1 mg−1and kcat of 231.2 s−1. The hydrolysis of linalyl acetate were carried out using ThLip1 and ThLip2 as catalyst, affording linalool yields over 140 mg/l in 10 h. •Two novel thermostable esterases were successfully hetero-expressed in E. Coli containing a few specific properties.•Two esterases possessed high thermostability and catalytic efficiency.•Two esterases displayed a potential for bio-conversion of tertiary alcohol esters.