An In Silico Approach to Enzymatic Synthesis of Fucooligosaccharides Using α-L-Fucosidase from Thermotoga maritima

Abstract: Fucooligosaccharides comprise the primary group of human milk oligosaccharides. Due to their beneficial properties, a series of synthetic methods have been proposed to obtain them. Enzy- matic methods show great promise, and α-L-fucosidase from Thermotoga maritima has emerged as a powerful catalyst for their production. Nonetheless, the enzyme’s limited substrate scope has de- layed its wider application. The present work aims to compare the relative reactivity of fucose, pNP-fucose, and ethyl-fucose, while also exploring the molecular interactions of these fucosyl-donors with the enzyme through a combination DFT and docking analysis. The HOMO-LUMO band gaps range from −7.14571 to −4.24429 eV, with α/β-pNP-fucose and α-fucose being the three most reactive compounds. Moderate association energies between −6.4 to −5.5 kcal·mol−1 were found in the dock- ing analysis, with α-pNP-fucose and both anomers of ethyl-fucose demonstrating the poorest affinity. In the case of α/β-lactose affinity to the β-fucose/enzyme complex, no significant differ- ences were shown. We conclude that the best fucosyl-donors for transfucosylation are those that maintain an enzyme affinity and reactivity similar to pNP-fucose

Síntesis electroquímica y evaluación de materiales electrocatalíticos a base de Cu, Co, y Cu-Co.

La búsqueda de fuentes alternas de energía a las de combustibles fósiles motiva el desarrollo de nuevos dispositivos altamente eficientes que permitan satisfacer la demanda energética actual y futura. En este sentido, las celdas de combustible pueden proporcionar esta energía alterna mediante un proceso de oxidación del combustible que las alimenta. Las celdas de combustible operan mediante una celda electroquímica de dos electrodos, un ánodo y un cátodo separados por un electrolito

An In Silico Approach to Enzymatic Synthesis of Fucooligosaccharides Using α-l-Fucosidase from Thermotoga maritima

Fucooligosaccharides comprise the primary group of human milk oligosaccharides. Due to their beneficial properties, a series of synthetic methods have been proposed to obtain them. Enzymatic methods show great promise, and α-l-fucosidase from Thermotoga maritima has emerged as a powerful catalyst for their production. Nonetheless, the enzyme’s limited substrate scope has delayed its wider application. The present work aims to compare the relative reactivity of fucose, pNP-fucose, and ethyl-fucose, while also exploring the molecular interactions of these fucosyl-donors with the enzyme through a combination DFT and docking analysis. The HOMO-LUMO band gaps range from −7.14571 to −4.24429 eV, with α/β-pNP-fucose and α-fucose being the three most reactive compounds. Moderate association energies between −6.4 to −5.5 kcal·mol−1 were found in the docking analysis, with α-pNP-fucose and both anomers of ethyl-fucose demonstrating the poorest affinity. In the case of α/β-lactose affinity to the β-fucose/enzyme complex, no significant differences were shown. We conclude that the best fucosyl-donors for transfucosylation are those that maintain an enzyme affinity and reactivity similar to pNP-fucose