Biochemical characterization of a new thermostable lipase from Bacillus pumilus strain

Researchers have identified a novel thermostable lipase from Bacillus pumilus, isolated from tannery waters in the Medina of Fez. This enzyme demonstrates exceptional thermal stability, retaining 60% of its activity after exposure to 100°C for 5 minutes and maintaining full activity at 70°C for 30 minutes. Unlike previously studied lipases, this enzyme exhibits non-inducible production and a molecular weight of 27 kDa, with optimal activity at pH 8 and 45°C. Its N-terminal amino acid sequence shows high homology with other Bacillus lipases, suggesting potential for biotechnological applications. The study employed PCR sequencing, gel filtration, and cation exchange chromatography to purify the enzyme and assess its biochemical properties.

Faouzi, F. L., el bergadi, f. e. b., Sayari, A. S., Elabed, S. E., Mohammed, I. M., Harchali, E. H. H., & Ibnsouda, S. K. I. (2015). Biochemical characterization of a new thermostable lipase from Bacillus pumilus strain. Turkish Journal of Biochemistry, 40(1), 8–14. https://doi.org/10.5505/tjb.2015.44227