Ginsenosides are the main compounds with pharmacological activities in ginseng. Deglycosylated ginsenosides, which are more pharmacologically active than glycosylated ginsenosides, can be produced by the specific or nonspecific hydrolysis of the sugar moieties in glycosylated ginsenosides using glycosidases. The enzymes that hydrolyze specifically ginsenosides with different types can be classified according to the enzymatic activity on the positions, inner and outer residues and types of sugar moieties in ginsenosides. Glycosylated ginsenosides are also hydrolyzed to deglycosylated ginsenosides with different hydrolytic pathways by cell conversion or fermentation. The biochemical properties of glycosidases involved in ginsenoside hydrolysis - ginsenosidases - were newly arranged and reviewed in accordance with different types. The combination of different-type ginsenosidases is suggested herein as an efficient tool to produce industrially important ginsenosides.

Diol synthase from Aspergillus nidulans was cloned and expressed in Escherichia coli. Recombinant E. coli cells expressing diol synthase from A. nidulans converted linoleic acid to a product that was identified as 5,8-dihydroxy-9,12(Z,Z)-octadecadienoic acid by liquid chromatography-mass spectrometry/mass spectrometry (LC-MS/MS). The recombinant cells and the purified enzyme showed the highest activity for linoleic acid among the fatty acids tested. The optimal reaction conditions for the production of 5,8-dihydroxy-9,12(Z,Z)-octadecadienoic acid from linoleic acid using whole recombinant E. coli cells expressing diol synthase were pH 7.5, 35°C, 250 rpm, 5 g l(-1) linoleic acid, 23 g l(-1) cells, and 20% (v/v) dimethyl sulfoxide in a 250-ml baffled flask. Under these optimized conditions, whole recombinant cells expressing diol synthase produced 4.98 g l(-1) 5,8-dihydroxy-9,12(Z,Z)-octadecadienoic acid for 150 min without detectable byproducts, with a conversion yield of 99% (w/w) and a productivity of 2.5 g l(-1) h(-1). This is the first report on the biotechnological production of dihydroxy fatty acid using whole recombinant cells expressing diol synthase.

The Platycodon grandiflorum root, Platycodi radix, a common vegetable, and its extract with glycosylated saponins, platycosides, have been used as food items and food health supplements for pulmonary diseases and respiratory disorders. Enzymes convert glycosylated saponins into deglycosylated saponins, which exhibit higher biological activity than glycosylated saponins. In this study, β-glucosidase from the hyperthermophilic bacterium Dictyoglomus turgidum converted platycosides in the Platycodi radix extract into deglucosylated platycosides. In addition, the enzyme completely converted platycoside E (PE), platycodin D3 (PD3), and platycodin D (PD) in Platycodi radix extract into deglucosylated platycodin D (deglu PD), which was first identified by nuclear magnetic resonance. The anti-inflammatory activities of deglu PD and deglucosylated Platycodi radix extract were higher than those of PE, PD3, PD, Platycodi radix extract, and baicalein, an anti-inflammatory agent. Therefore, deglucosylated Platycodi radix extract is expected to be used as improved functional food supplements.

The ginsenoside 20- O-β-glucopyranosyl-20( S)-protopanaxadiol, compound K, has attracted much attention in functional food, traditional medicine, and cosmetic industries because of diverse pharmaceutical activities. The effective production of compound K from ginseng extracts has been required. However, an enzyme capable of completely converting all protopanaxadiol (PPD)-type ginsenosides to compound K has not been reported until now. In this study, unlike other enzymes, β-glucosidase from Caldicellulosiruptor bescii was able to hydrolyze sugar moieties such as l-arabinofuranose as well as d-glucose and l-arabinopyranose as the C-20 outer sugar in ginsenosides. Thus, ginsenoside Rc containing l-arabinofuranose can be converted to compound K by only this enzyme. Under the optimized reaction conditions, the enzyme completely converted PPD-type ginsenosides in ginseng extracts to compound K with the highest productivity among the reported results. This is the first report of the enzyme capable of completely converting all PPD-type ginsenosides into compound K.

The generally recognized as safe microorganism Corynebacterium glutamicum expressing Geobacillus thermodenitrificans d-galactose isomerase (d-GaI) was an efficient host for the production of d-tagatose, a functional sweetener. The d-tagatose production at 500 g/L d-galactose by the host was 1.4-fold higher than that by Escherichia coli expressing d-GaI. The d-tagatose-producing activity of permeabilized C. glutamicum (PCG) cells treated with 1% (w/v) Triton X-100 was 2.1-fold higher than that of untreated cells. Permeabilized and immobilized C. glutamicum (PICG) cells in 3% (w/v) alginate showed a 3.1-fold longer half-life at 50 °C and 3.1-fold higher total d-tagatose concentration in repeated batch reactions than PCG cells. PICG cells, which produced 165 g/L d-tagatose after 3 h, with a conversion of 55% (w/w) and a productivity of 55 g/L/h, showed significantly higher d-tagatose productivity than that reported for other cells. Thus, d-tagatose production by PICG cells may be an economical process to produce food-grade d-tagatose.