Characterization of 6-O-α- rhamnosyl-β- glucosidase from Sarocladium strictum with focus on transglycosylation activity toward potential application as antitumor therapies.

GONZALEZ ALINA L; WEIZ, GISELA; MOLEJON, MARIA I; BRECCIA JAVIER D

Congreso; 15th International Symposium on Biocatalysis and Biotransformations (Biotrans 2021).; 2021

α-L-rhamnosyl-β-D-glucosidases are diglycosidases that catalyze the cleavage of the glycosidic bond between the aglycone and the disaccharide rutinose (α-L-rhamnopyranosyl-(1→6)-β-D- glucopyranose) of specific flavonoid glycosides [1]. Some α-L-rhamnosyl-β-D-glucosidases exhibit transglycosylation activities which provide an approach for obtaining novel rutinosylated molecules with enhanced capacities. These rutinosides could exhibit novel biological and biomedical activities [2]. Specifically, the presence of rhamnose as terminal unit of the rutinosides can change the pharmacokinetic properties of compounds as therapeutic agents [3]. Rhamnose-capped molecules appear to be resistant to hydrolysis in human tissues due to the absence of endogenous rutinosidases and α-L- rhamnosidases which would normally hydrolyze the respective glycosidic bonds. Thus, the rhamnose-capped molecules target specifically the sites where L-rhamnose receptors are located. This is an interesting strategy for enhancing the antitumoral effects of drugs [4].