Component

Saccharomyces cerevisiae alpha-glucosidase assay enzyme

Saccharomyces cerevisiae alpha-glucosidase assay enzyme. Interpret through the linked experimental species, preparation, compartment and exposure; no universal causal effect is implied.

4 recorded relationships. Experimental role, claim status and evidence remain attached to each record.

Read recorded mechanisms Open recursive mind map

How nutrients influence it

Every nutrient with a recorded effect on this component, credited to the nutrient that acted rather than the chapter that recorded it. Open a nutrient to see the findings and the conditions they were measured under.

How nutrients reach it in more than one step

Chains of two or more recorded steps that end here, grouped by the nutrient they start from. Each step is a separate finding, so a chain is a route a mechanism could take, not proof that it does.

Tracing routes…

What it does

Every recorded relationship this component is part of, grouped by its role. Plain wording comes first; the technical statement follows.

Recorded relationships

What acts on it

  1. Delphinidin 3,5-diglucoside showed no detected yeast alpha-glucosidase inhibition in the tested range.

    Delphinidin 3,5-O-diglucoside / delphin → Saccharomyces cerevisiae alpha-glucosidase assay enzyme source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Full text retrieved; relevant methods/results/figure text reviewed. No independent raw-data verification.
    experimental_contrast
    {"intervention": "Delphinidin 3,5-diglucoside concentration series", "comparator": "No inhibitor", "endpoint": "Delphinidin 3,5-diglucoside showed no detected yeast alpha-glucosidase inhibition in the tested range.", "effect_direction": "no_detected_change", "combination": "single", "conditions": []} Explicit extracted experimental comparison; source-derived draft.
    experimental_model
    Yeast alpha-glucosidase synthetic-substrate assay.
    interpretation_status
    Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.
    limitations
    Assay-specific null; not every digestive enzyme or unlimited concentrations.
    plain_language
    Delphinidin 3,5-diglucoside showed no detected yeast alpha-glucosidase inhibition in the tested range.
    primary_references
    Investigation of Anthocyanidins and Anthocyanins for Targeting α-Glucosidase in Diabetes Mellitus. | 2020 | DOI 10.3746/pnf.2020.25.3.263 | PMID 33083375 | https://pubmed.ncbi.nlm.nih.gov/33083375/ | https://pmc.ncbi.nlm.nih.gov/articles/PMC7541926/ | https://doi.org/10.3746/pnf.2020.25.3.263
    source_locator
    Reviewed reference lines 80-80; exact primary location described in quoted passage where extracted.

    Anthocyanins: detailed mechanisms of action (reviewed 4 October 2026) · lines 80–80

    Original AI-assisted review of primary studies and, where relevant, official regulatory records. Access level is retained per claim. Corrections, null results and unresolved questions remain explicit. Not publisher full text or independent replication. · supports · Yeast alpha-glucosidase synthetic-substrate assay. · source_derived_draft · unverified_draft

    **Enzyme identity changes the digestive-enzyme claim.** A purified-compound assay used yeast α-glucosidase and a synthetic substrate, not human sucrase-isomaltase. Delphinidin aglycone inhibited with an IC50 near 4.11 µM; cyanidin was about 17.01 µM. Delphinidin-3-glucoside was much weaker, around 364 µM, and its 3,5-diglucoside showed no detected inhibition in the tested range. These values establish structure-dependent assay behavior. They cannot be imported as human intestinal IC50 values or a clinical comparison with acarbose. Docking does not repair that species/substrate gap. [Promyos et al., 2020](https://pmc.ncbi.nlm.nih.gov/articles/PMC7541926/).
    Complete structured claim and evidence

  2. cyanidin inhibited yeast alpha-glucosidase in the synthetic-substrate assay; IC50 approximately 17.01 uM.

    Cyanidin → Saccharomyces cerevisiae alpha-glucosidase assay enzyme source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Full text retrieved; relevant methods/results/figure text reviewed. No independent raw-data verification.
    experimental_contrast
    {"intervention": "Purified cyanidin concentration series", "comparator": "Assay without inhibitor", "endpoint": "cyanidin inhibited yeast alpha-glucosidase in the synthetic-substrate assay; IC50 approximately 17.01 uM.", "effect_direction": "decrease", "combination": "single", "conditions": []} Explicit extracted experimental comparison; source-derived draft.
    experimental_model
    Saccharomyces cerevisiae alpha-glucosidase, pNPG substrate, pH 6, 37 C.
    interpretation_status
    Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.
    limitations
    Yeast enzyme assay; not human sucrase-isomaltase or maltase. IC50 depends on substrate and conditions; docking is not a human-target validation.
    plain_language
    cyanidin inhibited yeast alpha-glucosidase in the synthetic-substrate assay; IC50 approximately 17.01 uM.
    primary_references
    Investigation of Anthocyanidins and Anthocyanins for Targeting α-Glucosidase in Diabetes Mellitus. | 2020 | DOI 10.3746/pnf.2020.25.3.263 | PMID 33083375 | https://pubmed.ncbi.nlm.nih.gov/33083375/ | https://pmc.ncbi.nlm.nih.gov/articles/PMC7541926/ | https://doi.org/10.3746/pnf.2020.25.3.263
    source_locator
    Reviewed reference lines 80-80; exact primary location described in quoted passage where extracted.

    Anthocyanins: detailed mechanisms of action (reviewed 4 October 2026) · lines 80–80

    Original AI-assisted review of primary studies and, where relevant, official regulatory records. Access level is retained per claim. Corrections, null results and unresolved questions remain explicit. Not publisher full text or independent replication. · supports · Saccharomyces cerevisiae alpha-glucosidase, pNPG substrate, pH 6, 37 C. · source_derived_draft · unverified_draft

    **Enzyme identity changes the digestive-enzyme claim.** A purified-compound assay used yeast α-glucosidase and a synthetic substrate, not human sucrase-isomaltase. Delphinidin aglycone inhibited with an IC50 near 4.11 µM; cyanidin was about 17.01 µM. Delphinidin-3-glucoside was much weaker, around 364 µM, and its 3,5-diglucoside showed no detected inhibition in the tested range. These values establish structure-dependent assay behavior. They cannot be imported as human intestinal IC50 values or a clinical comparison with acarbose. Docking does not repair that species/substrate gap. [Promyos et al., 2020](https://pmc.ncbi.nlm.nih.gov/articles/PMC7541926/).
    Complete structured claim and evidence

  3. delphinidin inhibited yeast alpha-glucosidase in the synthetic-substrate assay; IC50 approximately 4.11 uM.

    Delphinidin → Saccharomyces cerevisiae alpha-glucosidase assay enzyme source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Full text retrieved; relevant methods/results/figure text reviewed. No independent raw-data verification.
    experimental_contrast
    {"intervention": "Purified delphinidin concentration series", "comparator": "Assay without inhibitor", "endpoint": "delphinidin inhibited yeast alpha-glucosidase in the synthetic-substrate assay; IC50 approximately 4.11 uM.", "effect_direction": "decrease", "combination": "single", "conditions": []} Explicit extracted experimental comparison; source-derived draft.
    experimental_model
    Saccharomyces cerevisiae alpha-glucosidase, pNPG substrate, pH 6, 37 C.
    interpretation_status
    Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.
    limitations
    Yeast enzyme assay; not human sucrase-isomaltase or maltase. IC50 depends on substrate and conditions; docking is not a human-target validation.
    plain_language
    delphinidin inhibited yeast alpha-glucosidase in the synthetic-substrate assay; IC50 approximately 4.11 uM.
    primary_references
    Investigation of Anthocyanidins and Anthocyanins for Targeting α-Glucosidase in Diabetes Mellitus. | 2020 | DOI 10.3746/pnf.2020.25.3.263 | PMID 33083375 | https://pubmed.ncbi.nlm.nih.gov/33083375/ | https://pmc.ncbi.nlm.nih.gov/articles/PMC7541926/ | https://doi.org/10.3746/pnf.2020.25.3.263
    source_locator
    Reviewed reference lines 80-80; exact primary location described in quoted passage where extracted.

    Anthocyanins: detailed mechanisms of action (reviewed 4 October 2026) · lines 80–80

    Original AI-assisted review of primary studies and, where relevant, official regulatory records. Access level is retained per claim. Corrections, null results and unresolved questions remain explicit. Not publisher full text or independent replication. · supports · Saccharomyces cerevisiae alpha-glucosidase, pNPG substrate, pH 6, 37 C. · source_derived_draft · unverified_draft

    **Enzyme identity changes the digestive-enzyme claim.** A purified-compound assay used yeast α-glucosidase and a synthetic substrate, not human sucrase-isomaltase. Delphinidin aglycone inhibited with an IC50 near 4.11 µM; cyanidin was about 17.01 µM. Delphinidin-3-glucoside was much weaker, around 364 µM, and its 3,5-diglucoside showed no detected inhibition in the tested range. These values establish structure-dependent assay behavior. They cannot be imported as human intestinal IC50 values or a clinical comparison with acarbose. Docking does not repair that species/substrate gap. [Promyos et al., 2020](https://pmc.ncbi.nlm.nih.gov/articles/PMC7541926/).
    Complete structured claim and evidence

  4. delphinidin-3-glucoside inhibited yeast alpha-glucosidase in the synthetic-substrate assay; IC50 approximately 364 uM.

    Delphinidin 3-O-beta-D-glucopyranoside → Saccharomyces cerevisiae alpha-glucosidase assay enzyme source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Full text retrieved; relevant methods/results/figure text reviewed. No independent raw-data verification.
    experimental_contrast
    {"intervention": "Purified delphinidin-3-glucoside concentration series", "comparator": "Assay without inhibitor", "endpoint": "delphinidin-3-glucoside inhibited yeast alpha-glucosidase in the synthetic-substrate assay; IC50 approximately 364 uM.", "effect_direction": "decrease", "combination": "single", "conditions": []} Explicit extracted experimental comparison; source-derived draft.
    experimental_model
    Saccharomyces cerevisiae alpha-glucosidase, pNPG substrate, pH 6, 37 C.
    interpretation_status
    Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.
    limitations
    Yeast enzyme assay; not human sucrase-isomaltase or maltase. IC50 depends on substrate and conditions; docking is not a human-target validation.
    plain_language
    delphinidin-3-glucoside inhibited yeast alpha-glucosidase in the synthetic-substrate assay; IC50 approximately 364 uM.
    primary_references
    Investigation of Anthocyanidins and Anthocyanins for Targeting α-Glucosidase in Diabetes Mellitus. | 2020 | DOI 10.3746/pnf.2020.25.3.263 | PMID 33083375 | https://pubmed.ncbi.nlm.nih.gov/33083375/ | https://pmc.ncbi.nlm.nih.gov/articles/PMC7541926/ | https://doi.org/10.3746/pnf.2020.25.3.263
    source_locator
    Reviewed reference lines 80-80; exact primary location described in quoted passage where extracted.

    Anthocyanins: detailed mechanisms of action (reviewed 4 October 2026) · lines 80–80

    Original AI-assisted review of primary studies and, where relevant, official regulatory records. Access level is retained per claim. Corrections, null results and unresolved questions remain explicit. Not publisher full text or independent replication. · supports · Saccharomyces cerevisiae alpha-glucosidase, pNPG substrate, pH 6, 37 C. · source_derived_draft · unverified_draft

    **Enzyme identity changes the digestive-enzyme claim.** A purified-compound assay used yeast α-glucosidase and a synthetic substrate, not human sucrase-isomaltase. Delphinidin aglycone inhibited with an IC50 near 4.11 µM; cyanidin was about 17.01 µM. Delphinidin-3-glucoside was much weaker, around 364 µM, and its 3,5-diglucoside showed no detected inhibition in the tested range. These values establish structure-dependent assay behavior. They cannot be imported as human intestinal IC50 values or a clinical comparison with acarbose. Docking does not repair that species/substrate gap. [Promyos et al., 2020](https://pmc.ncbi.nlm.nih.gov/articles/PMC7541926/).
    Complete structured claim and evidence

In the sources

Preserved passages that mention this component, quoted exactly. Open one to read it in context.

    This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.