2026-06-27T23:21:30Zhttps://docta.ucm.es/rest/oai/request

oai:docta.ucm.es:20.500.14352/916182025-03-18T15:57:54Zcom_20.500.14352_14col_20.500.14352_15

Trobo Maseda, Lara Romero Fernandez, Maria Guisan, Jose Rocha Martín, Javier 2023-12-20T15:53:06Z 2023-12-20T15:53:06Z 2023 Trobo-Maseda, Lara, et al. «Glycosylation of Polyphenolic Compounds: Design of a Self-Sufficient Biocatalyst by Co-Immobilization of a Glycosyltransferase, a Sucrose Synthase and the Cofactor UDP». International Journal of Biological Macromolecules, vol. 250, octubre de 2023, p. 126009. https://doi.org/10.1016/j.ijbiomac.2023.126009. 0141-8130 10.1016/j.ijbiomac.2023.126009 https://hdl.handle.net/20.500.14352/91618 1879-0003 https://doi.org/10.1016/j.ijbiomac.2023.126009 Glycosyltransferases catalyze the regioselective glycosylation of polyphenolic compounds, increasing their solubility without altering their antioxidant properties. Leloir-type glycosyltransferases require UDP-glucose as a cofactor to glycosylate a hydroxyl of the polyphenol, which is expensive and unstable. To simplify these processes for industrial implementation, the preparation of self-sufficient heterogeneous biocatalysts is needed. In this study, a glycosyltransferase and a sucrose synthase (as an UDP-regenerating enzyme) were co-immobilized onto porous agarose-based supports coated with polycationic polymers: polyethylenimine and polyallylamine. In addition, the UDP cofactor was strongly ionically adsorbed and co-immobilized with the enzymes, eliminating the need to add it separately. Thus, the optimal self-sufficient heterogeneous biocatalyst was able to catalyze the glycosylation of three polyphenolic compounds (piceid, phloretin and quercetin) with in situ regeneration of the UDP-glucose, allowing multiple consecutive reaction cycles without the addition of exogenous cofactor. A TTN value of 50 (theoretical maximum) was obtained in the reaction of piceid glycosylation, after 5 reaction cycles, using the self-sufficient biocatalyst based on an improved sucrose synthase variant. This result was 5-fold higher than the obtained using soluble cofactor and the co-immobilized enzymes, and much higher than those reported in the literature for similar processes. eng http://creativecommons.org/licenses/by/4.0/ open access Attribution 4.0 International Glycosylation of polyphenolic compounds: design of a self-sufficient biocatalyst by co-immobilization of a glycosyltransferase, a sucrose synthase and the cofactor UDP journal article