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PMID:24475050

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Citation

Cui, CH, Kim, JK, Kim, SC and Im, WT (2014) Characterization of a ginsenoside-transforming β-glucosidase from Paenibacillus mucilaginosus and its application for enhanced production of minor ginsenoside F₂. PLoS ONE 9:e85727

Abstract

A novel β-glucosidase (BglPm) was identified from Paenibacillus mucilaginosus KCTC 3870(T) which has ginsenoside converting activity. The gene, termed bglPm, consists of 1,260 bp and belongs to glycoside hydrolase family 1 (GH1). After being overexpressed and purified from Escherichia coli, the enzymatic properties of BglPm were investigated. The enzyme exhibited an optimal activity at 45°C and pH 7.5 and showed high bioconversion ability for major ginsenoside Rb1 and Rd into ginsenoside F2. Thus, it was used for mass production of relatively high pure F2 from relatively abundant protopanaxadiol type ginsenosides mixture (PPDGM) with combined usage of ginsenoside Rc-hydrolyzing enzyme. Scale-up of production using 250 g of the PPDGM resulted in 152 g of F2 with 80.1% chromatography purity and 95.7% recovery. These results suggest that this enzyme would be useful in the preparation of pharmacologically active ginsenoside F2 in the functional food and pharmaceutical industries.

Links

PubMed PMC3903488 Online version:10.1371/journal.pone.0085727

Keywords

Biotechnology/methods; Chromatography, High Pressure Liquid; Chromatography, Thin Layer; Cloning, Molecular; DNA Primers/genetics; Ginsenosides/biosynthesis; Ginsenosides/metabolism; Hydrogen-Ion Concentration; Kinetics; Paenibacillus/enzymology; Temperature; beta-Glucosidase/genetics; beta-Glucosidase/metabolism

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

PAEMK:F8FFH2

GO:0015926: glucosidase activity

ECO:0000314:

F

Figure 4 shows the conversion of different types of ginsenosides into the F2 type by hydrolysis of a glucosyl group by BglPm. Figure 5 shows the pathway

complete
CACAO 10822

Notes

See also

References

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