A novel GH1 β-glucosidase Fpglu1 from Fervidobacterium pennivorans DSM9078 was successfully cloned and expressed in Escherichia coli. This hyperthermophilic enzyme possesses unique features that make it valuable in biochemistry and pharmacology. It exhibited optimal activity at temperatures exceeding 100 °C, a trait rarely observed in other enzymes, and demonstrated extraordinary thermostability. It displayed multifunctional activity, with the highest activity observed for p-nitrophenyl-β-d-glucopyranoside (pNPGlu) at 92.47 U/mg. Furthermore, the distinctive capacity of Fpglu1 to transform ginsenosides (Rb1, Rb2, and Rc) into Compound-K (C-K) sets it apart from the other enzymes. It effectively cleaved the external β-(1-6) glycosidic linkage at the C-20 position of ginsenosides Rb1, Rb2, and Rc, followed by hydrolysis ofthe internal glycosidic bond connected to the C-3 position. The k