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A Novel Ginsenoside-Transforming α-L-Rhamnosidase from Bifidobacterium: Screening, Characterization and Application
Chang-Hao Cui1, Doohang Shin1, Byung-Serk Hurh1
1Sempio Fermentation Research Center, Sempio Foods Company, Osong 28156, Republic of Korea.
Biomolecules
|January 8, 2025
Summary
A novel rhamnosidase (C118) from Bifidobacterium efficiently transforms ginsenoside Re. This enzyme shows enhanced thermal stability and activity compared to previous rhamnosidases, with significant implications for producing valuable ginsenosides.
Area of Science:
- Biotechnology
- Enzymology
- Microbiology
Background:
- Ginsenoside-transforming rhamnosidases are crucial for modifying ginsenosides but remain underexplored.
- Existing research lacks sufficient understanding of rhamnosidase enzymes for ginsenoside transformation.
- There is a need for efficient and stable rhamnosidases for industrial applications.
Purpose of the Study:
- To identify and characterize novel ginsenoside-transforming rhamnosidases.
- To evaluate the efficiency and properties of a newly discovered rhamnosidase (C118) from Bifidobacterium.
- To compare the performance of C118 with existing ginsenoside-transforming rhamnosidases.
Main Methods:
- Screening of eight putative rhamnosidases for ginsenoside transformation activity.
- Recombinant expression of the identified rhamnosidase (C118) in Escherichia coli.
- Enzyme characterization including optimal pH, temperature, thermal stability, and kinetic analysis (k/K values).
- Structural prediction analysis to understand enzyme-substrate interactions.
Main Results:
- A novel α-L-rhamnosidase, C118 from Bifidobacterium, was identified with high efficiency in hydrolyzing ginsenoside Re.
- C118 demonstrated optimal activity at pH 6.0 and 45 °C, with superior thermal stability compared to BD890.
- The k/K value of C118 was 1.45 times higher than BD890, and it completely converted ginsenoside Re in a mixture within 12 hours.
Conclusions:
- The novel rhamnosidase C118 represents the most efficient ginsenoside Re-transforming enzyme reported to date.
- Structural insights suggest a role for hydrophobic areas in enzyme activity, advancing understanding of rhamnosidase-substrate interactions.
- These findings hold significant potential for improving the production of pharmacologically active ginsenosides for various industries.
