| Full text | |
| Author(s): |
Maria, Taina Carolini
;
Pereira, Pamela A. Maldaner
;
Pepe, Elisangela Soares Gomes
;
Lemos, Eliana Gertrudes de Macedo
Total Authors: 4
|
| Document type: | Journal article |
| Source: | International Journal of Biological Macromolecules; v. 297, p. 12-pg., 2025-01-16. |
| Abstract | |
This study characterized a novel bacterial lipase with high biotechnological potential, focusing on industrial and environmental applications. Bacterial isolates were screened using olive oil as a substrate, and the strain with the highest hydrolytic halo was identified as Burkholderia sp. via 16S rRNA analysis. The secreted lipase was purified and exhibited high hydrolytic activity, specifically targeting long-chain fatty acids. Gas chromatography analyses confirmed its ability to hydrolyze fatty acids present in olive oil, while kinetic parameters and substrate preferences were assessed using synthetic substrates. Optimal activity was observed at pH 4.5 and temperatures between 40 and 60 degrees C. The enzyme demonstrated remarkable thermal stability, retaining over 78 % residual activity after 24 h at 30, 40, 60, and even 70 degrees C. It also displayed broad pH stability, with increased relative activity at pH 6.5 over time. LipBK showed resilience in the presence of metallic ions, salts, EDTA, and non-ionic detergents, with enhanced activity in the presence of additives like KCl, CaCl2, and Triton X-100. These properties highlight its robustness and suitability for applications in acidic and thermally variable environments, such as biodiesel production, waste treatment, and sustainable industrial processes, contributing to global sustainability goals. (AU) | |
| FAPESP's process: | 19/13493-1 - Prospecting, functional and structural characterization of lipolytic enzymes of marine metagenomes |
| Grantee: | Eliana Gertrudes de Macedo Lemos |
| Support Opportunities: | Regular Research Grants |