Role of glycosidases in the membranlytic, antifungal action of Saponins.
In studies on the membranlytic action of various saponins on mycelium of Botrytis cinerea and Rhizoctonia solani digitonin, alpha-hederin and tomatin caused considerable leakage of free amino acids, while aescin and theasaponin were less effective. Cyclamin significantly damaged cell membranes of R. solani, but did not change the selective permeability of B. cinerea. Cell membrane disruption was accompanied by an enzymatic conversion of saponins into their corresponding aglycones in cell membrane vicinity, an effect which was significantly inhibited by aldonolactones, known inhibitors of beta-glycosidases. These results lead to the conclusion that the hardly water soluble aglycones are the active part of the saponin molecules, the saponins themselves being only water soluble transport forms. It follows, that the presence of appropriate glycosidases in cell membranes, capable of converting saponins into their aglycones, is a prerequisite for the membranlytic action of saponins. The similarity of the membranlytic effects of saponins towards fungi and erythrocytes is descussed.
D002462:Cell Membrane / Q000187:drug effects* / Q000201:enzymology; D005658:Fungi / Q000187:drug effects* / Q000201:enzymology; D005696:Galactosidases / Q000378:metabolism; D005959:Glucosidases / Q000378:metabolism; D006026:Glycoside Hydrolases / Q000378:metabolism*; D006868:Hydrolysis; D003904:Mitosporic Fungi / Q000187:drug effects; D012232:Rhizoctonia / Q000187:drug effects; D012503:Saponins / Q000494:pharmacology*
D012503:Saponins; D005696:Galactosidases; D005959:Glucosidases; D006026:Glycoside Hydrolases