How the Triton X-100 modulates the activity/stability of the Thermomyces lanuginose lipase: Insights from experimental and molecular docking approaches

• Published in: International journal of biological macromolecules 2018-12, Vol.120 (Pt B), p.2410-2417
• Main Authors: Mesa, Monica, Pereañez, Jaime Andres, Preciado, Lina María, Bernal, Claudia
• Format: Article
• Language: English
• Subjects: Catalytic Domain; Catalytic performance; Enzyme Stability - drug effects; Enzymes, Immobilized - chemistry; Enzymes, Immobilized - metabolism; Eurotiales - enzymology; Hydrogen-Ion Concentration; Lipase - chemistry; Lipase surfactant interactions; Molecular Docking Simulation; Octoxynol - chemistry; Octoxynol - pharmacology; Secondary structure
• ISSN: 0141-8130; 1879-0003
• DOI: 10.1016/j.ijbiomac.2018.09.009

The lipase and Triton X-100 mixture is common for stabilization, immobilization and application processes of these kinds of enzymes. The objective of this article was to study the structural behavior and catalytic performance of Thermomyces lanuginose lipase in the presence of Triton X-100 at 25 °C and different pHs. The structural changes were followed by circular dichroism, correlating them with the catalytic performance, which is reported as the initial lipase activity in the hydrolysis of p‑nitro phenyl butyrate at zero time and residual activity after 48 h of incubation in the absence or presence of surfactant, at the selected pHs. Computational simulations allowed to explain the correlations between the physicochemical changes and the formation of surfactant protein complex, leading to the elucidation of the main interactions that drive activity and stability of this lipase in presence of the Triton X-100 surfactant. Main results showed the Triton X-100-enzyme complex modulates the site active geometry, favoring a better substrate-enzyme adjustment, which influences the activity and stability at evaluated pHs. This study contributes to understand the effect of some additives commonly used to improve the biocatalytic performance on several applications for different industrial fields. The enzyme-surfactant interactions are well drawn in this work from experimental and computational approaches, for TLL and Triton X-100 system at selected pHs. Taking into account the similar nature of the enzyme substrate (p‑NPB) and Triton X-100, a competence between them can be hypothesized, which highlights the main role of the Triton X-100 on the activity/stability of TLL instead of the pH effect. [Display omitted] •Triton X-100 and pH effects on TLL structure/activity/stability relationship•p‑Nitrophenol butyrate/lipase and Triton X-100/lipase docking studies in TLL enzyme•Experimental and computational correlation to understand changes on enzyme performance•Comprehension of surfactant-enzyme interactions for developing stabilizing strategies