The ginsenoside Rg₂(S), which is one of the pharmaceutical components of ginseng, is known to have neuroprotective, anti-inflammation, and anti-diabetic effects. However, the usage of ginsenoside Rg₂(S) is restricted owing to the small amounts found in white and red ginseng. To enhance the production of ginsenoside Rg₂(S) as a 100 gram unit with high specificity, yield, and purity, an enzymatic bioconversion method was developed to adopt the recombinant glycoside hydrolase (BglPC28), which is a ginsenoside-transforming recombinant β-glucosidase from Pseudonocardia sp. strain Gsoil 1536. The gene, termed bglPC28, encoding β-glucosidase (BglPC28) belonging to the glycoside hydrolase family 3 was cloned. bglPC28 consists of 2,232 bp (743 amino acid residues) with a predicted molecular mass of 78,975 Da. This enzyme was overexpressed in Escherichia coli BL21(DE3) using a GST-fused pGEX 4T-1 vector system. The optimum conditions of the recombinant BglPC28 were pH 7.0 and 37°C. BglPC28 can effectively transform the ginsenoside Re to Rg₂(S); the K_m values of PNPG and Re were 6.36±1.10 and 1.42±0.13 mM, respectively, and the V_max values were 40.0±2.55 and 5.62±0.21 µmol min⁻¹ mg⁻¹ of protein, respectively. A scaled-up biotransformation reaction was performed in a 10 L jar fermenter at pH 7.0 and 30°C for 12 hours with a concentration of 20 mg/ml of ginsenoside Re from American ginseng roots. Finally, 113 g of Rg₂(S) was produced from 150 g of Re with 84.0±1.1% chromatographic purity. These results suggest that this enzymatic method could be usefully exploited in the preparation of ginsenoside Rg₂(S) in the cosmetics, functional food, and pharmaceutical industries.

Two novel strains, designated KTCe-2T and 7C-9T, isolated from an activated sludge and freshwater sediment, respectively in South Korea, were characterized by a polyphasic approach to clarify their taxonomic positions. Phylogenetic analysis based on 16S rRNA gene sequences indicated that both isolates belong to the genus Lysobacter and are most closely related to ‘Lysobacter daecheongensis’ Dae 08 (98.5 % and 97.6 % similarity for strains KTCe-2T and 7C-9T, respectively), Lysobacter brunescens KCTC 12130T (98.4 % and 97.2 %), and Lysobacter oligotrophicus JCM 18257T (97.1 % and 96.8 %). The G+C content of the genomic DNA of strains KTCe-2T and 7C-9T was 68.6 % and 71.5 mol%, respectively. Strains KTCe-2T and 7C-9T possessed ubiquinone-8 as the sole respiratory quinone, and a fatty acid profile with iso-C15 : 0 and iso-C16 : 0 as the major fatty acids supported the affiliation of the two strains to the genus Lysobacter. Moreover, the physiological and biochemical results and low DNA–DNA relatedness values allowed the phenotypic and genotypic differentiation of strains KTCe-2T and 7C-9T from other species of the genus Lysobacter with validly published names. Therefore, the two isolates represent two novel species of the genus Lysobacter, for which the name Lysobacter hankyongensis sp. nov. (type strain KTCe-2T = JCM 18204T = KACC 16618T) and Lysobacter sediminicola sp. nov. (type strain 7C-9T = JCM 18205T = KACC 16617T) are proposed.

Minor ginsenosides, such as compound K, Rg₃(S), which can be produced by deglycosylation of ginsenosides Rb₁, showed strong anti-cancer effects. However, the anticancer effects of gypenoside LXXV, which is one of the deglycosylated shapes of ginsenoside Rb₁, is still unknown due to the rarity of its content in plants. Here, we cloned and characterized a novel ginsenoside-transforming β-glucosidase (BglG167b) derived from Microbacterium sp. Gsoil 167 which can efficiently hydrolyze gypenoside XVII into gypenoside LXXV, and applied it to the production of gypenoside LXXV at the gram-scale with high specificity. In addition, the anti-cancer activity of gypenoside LXXV was investigated against three cancer cell lines (HeLa, B16, and MDA-MB231) in vitro. Gypenoside LXXV significantly reduced cell viability, displaying an enhanced anti-cancer effect compared to gypenoside XVII and Rb₁. Taken together, this enzymatic method would be useful in the preparation of gypenoside LXXV for the functional food and pharmaceutical industries.

Ginsenoside F1, a pharmaceutical component of ginseng, is known to have antiaging, antioxidant, anticancer, and keratinocyte protective effects. However, the usage of ginsenoside F1 is restricted owing to the small amount found in Korean ginseng. To enhance the production of ginsenoside F1 as a 10 g unit with high specificity, yield, and purity, an enzymatic bioconversion method was developed to adopt the commercial enzyme Cellulase KN from Aspergillus niger with food grade, which has ginsenoside-transforming ability. The proposed optimum reaction conditions of Cellulase KN were pH 5.0 and 50°C. Cellulase KN could effectively transform the ginsenosides Re and Rg1 into F1. A scaled-up biotransformation reaction was performed in a 10 L jar fermenter at pH 5.0 and 50°C for 48 h with protopanaxatriol-type ginsenoside mixture (at a concentration of 10 mg/mL) from ginseng roots. Finally, 13.0 g of F1 was produced from 50 g of protopanaxatriol-type ginsenoside mixture with 91.5 ± 1.1% chromatographic purity. The results suggest that this enzymatic method could be exploited usefully for the preparation of ginsenoside F1 to be used in cosmetic, functional food, and pharmaceutical industries.