Highly regioselective hydrolysis of the glycosidic bonds in ginsenosides catalyzed by snailase.

[Display omitted] • High regioselectivity and hydrolysis ability to ginsenosides by snailase were found. • Ginsenoside Ro was transformed to Chikusetsusaponin Ⅳa in vitro for the first time. • Ginsenoside Ro was transformed to Glucosyl oleanilate in vitro for the first time. • Ginsenoside Ro was transformed to Zingibroside R1 in vitro for the first time. • Ginsenoside Ro was transformed to Silphioside F in vitro for the first time. Minor ginsenosides display higher physiological activities than those of major ginsenosides, but their low abundance limits their clinical application. In this study, snailase was employed to transform protopanaxadiol-type (PPD) ginsenosides, protopanaxatriol-type (PPT) ginsenosides, and Ro to minor ginsenosides. The results showed that snailase hydrolyzed the saccharide chains at the C-3 position of Rb1, Rc, Rb2 Rg3 and Ro and the saccharide chains at the C-28 position of Ro efficiently. The end glucosyl unit of the saccharide chain at the C-6 position of Rf was hydrolyzed entirely. However, the rhamnosyl of Re was intact. The end glucosyl unit of the ginsenoside Rb1 was hydrolyzed entirely, but both arabinopyranosyl of Rb2 and arabinofuranosyl of Rc were not hydrolyzed. So snailase is selective for glycoside bond locations and saccharide types of ginsenoside, and it can be used to produce Rg3, CK, Rh1 and so on. [ABSTRACT FROM AUTHOR]