A Novel Ginsenoside-Transforming Enzyme from Bifidobacterium
Author Information
Author(s): Cui Chang-Hao, Shin Doohang, Hurh Byung-Serk, Im Wan-Taek, Menegazzi Marta, Piacente Sonia
Primary Institution: Sempio Fermentation Research Center, Sempio Foods Company
Hypothesis
The use of a novel rhamnosidase enzyme can significantly enhance the efficiency and specificity of the production process of ginsenoside Rg1 from ginsenoside Re.
Conclusion
The newly identified rhamnosidase C118 from Bifidobacterium efficiently converts ginsenoside Re into Rg1, demonstrating high specificity and potential for industrial applications.
Supporting Evidence
- The enzyme C118 was found to convert all ginsenoside Re in a mixture to Rg1 after 12 hours.
- C118 exhibited a kcat/Km value 1.45 times higher than the previously known enzyme BD890.
- The optimal activity of C118 was observed at pH 6.0 and 45 °C.
- C118 showed greater thermal stability compared to BD890.
- Structural predictions indicated that hydrophobic areas near the active site may enhance enzyme activity.
Takeaway
Scientists found a new enzyme that can change a substance in ginseng into a better version, which could help make medicines and health products.
Methodology
The study involved screening eight putative rhamnosidases, characterizing the most efficient enzyme (C118), and testing its ability to convert ginsenoside Re into Rg1 under various conditions.
Limitations
The study primarily focused on a single enzyme and its performance, which may not represent all potential rhamnosidases.
Digital Object Identifier (DOI)
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