Herein, a novel ginsenosidase, named ginsenosidase type IV, hydrolyzing 6-O-multi-glycosides of protopanaxatriol-type ginsenosides (PPT), such as Re, R1, Rf, and Rg2, was isolated from the Aspergillus sp. 39g strain, purified, and characterized. Ginsenosidase type IV was able to hydrolyze the 6-O-${alpha}$-L-($1{ ightarrow}2$)-rhamnoside of Re and the 6-O-${eta}$-D-($1{ ightarrow}2$)-xyloside of R1 into ginsenoside Rg1. Subsequently, it could hydrolyze the 6-O-${eta}$-D-glucoside of Rg1 into F1. Similarly, it was able to hydrolyze the 6-O-$_{alpha}$-L-($1{ ightarrow}2$)-rhamnoside of Rg2 and the 6-O-${eta}$-D-($1{ ightarrow}2$)-glucoside of Rf into Rh1, and then further hydrolyze Rh1 into its aglycone. However, ginsenosidase type IV could not hydrolyze the 3-O- or 20-O-glycosides of protopanaxadiol-type ginsenosides (PPD), such as Rb1, Rb2, Rb3, Rc, and Rd. These exhibited properties are significantly different from those of glycosidases described in Enzyme Nomenclature by the NC-IUBMB. The optimal temperature and pH for ginsenosidase type IV were $40^{circ}C$ and 6.0, respectively. The activity of ginsenosidase type IV was slightly improved by the $Mg^{2+}$ ion, and inhibited by $Cu^{2+}$ and $Fe^{2+}$ ions. The molecular mass of the enzyme, based on SDS-PAGE, was noted as being approximately 56 kDa.