ReviewFoods (Basel, Switzerland)2023
Progress in the Conversion of Ginsenoside Rb1 into Minor Ginsenosides Using β-Glucosidases.
Review in Foods (Basel, Switzerland), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers, 1 of them a synthesis that pooled it.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
16 citing papers in PubMed, 1 synthesis or guideline pooled it, 29 citations in OpenAlex.
- Ginseng Bioactive Components as Gut-Brain Axis-Targeted Modulators: Therapeutic Potential and Mechanisms in Multifactorial Diseases.Nutrients · 2026Pooled it
- Differential Biotransformation of Glycyrrhizin by Licorice-Derived Endophytic Fungi and Accumulation-Promoting Effects of Fungal Inoculation.International journal of molecular sciences · 2026Article
- The rise of dehydrated ginsenosides: phytochemistry and pharmacology.Journal of advanced research · 2026Review
- Bidirectional Fermentation ofFoods (Basel, Switzerland) · 2026Article
- Recent Progress in the Regioselective Biotransformation and Multitarget Therapeutic Potential of Ginsenoside Rd.Molecules (Basel, Switzerland) · 2026Review
- Ginsenosides in Modern Pharmaceutics: Mechanisms, Applications, Challenges, and Perspectives.Biomolecules · 2026Review
- Pharmacokinetic variability of 20(S)-protopanaxadiol-type ginsenosides Rb1, rd, and compound K from Korean red ginseng in experimental rodents.Scientific reports · 2025Article
- Comparison of the Transformation Ability of the Major Saponins inMicroorganisms · 2025Article
- Pharmacological Mechanism and Drug Research Prospects of Ginsenoside Rb1 as an Antidepressant.Antioxidants (Basel, Switzerland) · 2025Review
- Comparison in Bioactive Compounds and Antioxidant Activity ofFoods (Basel, Switzerland) · 2024Article
- Enhanced Minor Ginsenoside Contents of Nano-Sized Black Korean Ginseng through Hot Melt Extrusion.Materials (Basel, Switzerland) · 2024Article
- Impact of ginsenoside Rb1 on gut microbiome and associated changes in pharmacokinetics in rats.Scientific reports · 2024Article
- Engineered β-glycosidase from Hyperthermophilic Sulfolobus solfataricus with Improved Rd-hydrolyzing Activity for Ginsenoside Compound K Production.Applied biochemistry and biotechnology · 2024Article
- Characterization of a Novel Hyperthermophilic GH1 β-Glucosidase fromMicroorganisms · 2024Article
- Structural Characters and Pharmacological Activity of Protopanaxadiol-Type Saponins and Protopanaxatriol-Type Saponins from Ginseng.Advances in pharmacological and pharmaceutical sciences · 2024Review
- Transformation of Ginsenosides byMolecules (Basel, Switzerland) · 2023Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
In recent years, minor ginsenosides have received increasing attention due to their outstanding biological activities, yet they are of extremely low content in wild ginseng. Ginsenoside Rb1, which accounts for 20% of the total ginsenosides, is commonly used as a precursor to produce minor ginsenosides via β-glucosidases. To date, many research groups have used different approaches to obtain β-glucosidases that can hydrolyze ginsenoside Rb1. This paper provides a compilation and analysis of relevant literature published mainly in the last decade, focusing on enzymatic hydrolysis pathways, enzymatic characteristics and molecular mechanisms of ginsenoside Rb1 hydrolysis by β-glucosidases. Based on this, it can be concluded that: (1) The β-glucosidases that convert ginsenoside Rb1 are mainly derived from bacteria and fungi and are classified as glycoside hydrolase (GH) families 1 and 3, which hydrolyze ginsenoside Rb1 mainly through the six pathways. (2) Almost all of these β-glucosidases are acidic and neutral enzymes with molecular masses ranging from 44-230 kDa. Furthermore, the different enzymes vary widely in terms of their optimal temperature, degradation products and kinetics. (3) In contrast to the GH1 β-glucosidases, the GH3 β-glucosidases that convert Rb1 show close sequence-function relationships. Mutations affecting the substrate binding site might alter the catalytic efficiency of enzymes and yield different prosapogenins. Further studies should focus on elucidating molecular mechanisms and improving overall performances of β-glucosidases for better application in food and pharmaceutical industries.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.