Ginsenoside Rc(Nanjing University of Chinese Medicine)

α-L-Arabinofuranosidase has been widely used in the fields of enhancing pasta production quality, fruit juice clarification, enhancing wine flavor, increasing feed utilization rate, and developing special drug ingredients, playing a pivotal role in the food processing, feed, and medical care industries. In this study, a novel α-L-arabinofuranosidase (BpAbf51A), belonging to glycoside hydrolase family 51 (GH51), was cloned from the Bacillus pumilus strain 145 and expressed in Escherichia coli BL21 (DE3), with a molecular weight of approximately 56.0 kDa. BpAbf51A comprises two characteristic domains of the GH51 family: an N-terminal (β/α)₈-barrel catalytic domain and a C-terminal jelly-roll domain. The enzyme exhibits high substrate specificity for p-nitrophenyl-α-L-arabinofuranoside and demonstrates optimal catalytic activity at 50°C and pH 8.0, suggesting its potential for industrial applications under moderate conditions. Notably, BpAbf51A specifically hydrolyzes the arabinofuranosyl moiety at the C-20 position of ginsenoside Rc to produce ginsenoside Rd. Molecular docking and two-dimensional interaction diagrams further revealed that the key amino acid residues, Ser213 and Asn214 of BpAbf51A, form strong hydrogen bonds with ginsenoside Rc. In this study, a novel α-L-arabinofuranosidase, BpAbf51A, has demonstrated significant potential for industrial applications in the production of rare saponins and other glycoside-based natural products, providing new research directions for the development of efficient biocatalysts.

Ginsenoside Rc (gRc), a component of Panax ginseng, protects against muscle atrophy in in vitro and in vivo models; however, the underlying molecular mechanisms remain unclear. Through systematic transcriptomic analysis and docking simulation, we investigated these protective effects on muscle cells under oxidative stress. Pathway analysis revealed that gRc significantly suppressed oxidative stress-induced transforming growth factor-beta (TGF-β) signaling. Molecular docking indicated that gRc bound to TGF-β receptor 1 (TGFBR1), similar to known TGFBR1 inhibitors. Gene expression analysis identified nucleolin (Ncl), a downstream effector of TGF-β signaling, as a key target of gRc. Ncl silencing confirmed that gRc protected myotubes from degradation via the TGF-β-Ncl axis. Cross-sectional analysis of human muscle transcriptomic data demonstrated the relevance of targeting Ncl under muscle atrophy-related conditions. Overall, gRc alleviates oxidative stress-induced muscle atrophy by inhibiting TGF-β signaling and downregulating Ncl expression, highlighting its therapeutic potential.