Fucooligosaccharides, α-L-fucosidase, DFT study, molecular docking
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.
Pérez-Escalante, Emmanuel; González-Olivares, Luis Guillermo; Castañeda-Ovando, Araceli; Cruz-Guerrero, Alma Elizabeth; Trant, John F.; López-Orozco, Wendolyne; Mendoza-Huizar, Luis Humberto; and Alatorre-Santamaría, Sergio. (2020). An In Silico Approach to Enzymatic Synthesis of Fucooligosaccharides Using α-L-Fucosidase from Thermotoga maritima. Chemistry Proceedings, 3 (10).