Mogroside IV

This study examined the ability of sweet elements extracted from Siraitia grosvenori (SG) to inhibit the oxidation of LDL. We monitored the formation of conjugated diene during copper-mediated LDL oxidation in the presence or absence of sweet elements of whole extract of SG (SG extract) or cucurbitane glycosides (CGs) purified from SG extract as sweet elements. CGs consist of Mogroside IV (Mog.IV), Mogroside V (Mog.V), 11-Oxo-mogroside V (11-Oxo-mog.V), and Siamenoside I (Sia.I). In addition, the effect of these elements on human umbilical vein endothelial cell (HUVEC)- mediated LDL oxidation was tested by measuring production of lipid peroxides. SG extract inhibited copper-mediated LDL oxidation in a dose-dependent fashion, but neither glucose nor erythritol suppressed the oxidation. Among CGs, 11-Oxo-mog.V significantly inhibited LDL oxidation, and prolongation of the lag time during LDL oxidation by 11-Oxo-mog.V was dose-dependent. The lag time (119.7 +/- 8.9 min) in the presence of 200 microM 11-Oxo-mog.V was significantly longer than that (76.8 +/- 5.5 min) of control (p < 0.01). In addition, SG extract and 11-Oxo-mog.V inhibited HUVEC-mediated LDL oxidation in a dose-dependent manner. These results demonstrate that SG extract can inhibit LDL oxidation and that 11-Oxo-mog.V, a sweet element of SG extract, provides the anti-oxidative property of SG which might reduce the atherogenic potential of LDL.

Siraitia grosvenorii is a type of fruit used in traditional Chinese medicine. Previous studies have shown that the conversion of saponins was often carried out by chemical hydrolysis, which can be problematic because of the environmental hazards it may cause and the low yield it produces. Therefore, the purpose of this study is to establish a continuous bioreactor with immobilized enzymes to produce siamenoside I and mogroside IV. The results show that the immobilization process of β-glucosidase exhibited the best relative activity with a glutaraldehyde (GA) concentration of 1.5%, carrier activation time of 1 h and binding enzyme time of 12 h. After the immobilization through GA linkage, the highest relative activity of β-glucosidase was recorded through the reaction with the substrate at 60 °C and pH 5. Subsequently, the glass microspheres with immobilized β-glucosidase were filled into the reactor to maintain the optimal active environment, and the aqueous solution of Siraitia grosvenorii extract was introduced by controlling the flow rate. The highest concentration of siamenoside I and mogroside IV were obtained at a flow rate of 0.3 and 0.2 mL/min, respectively. By developing this immobilized enzyme system, siamenoside I and mogroside IV can be prepared in large quantities for industrial applications.