Identification of Corn Peptides with Alcohol Dehydrogenase Activating Activity Absorbed by Caco-2 Cell Monolayers.

Zhe Wang, Guanlong Li, Xiaolan Liu

Open access · goldAbstract read

In one paragraph

Article in Molecules (Basel, Switzerland), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it

0cells of the map it votes in

0citing papers in PubMed

1.7field-weighted citation impact, top 17% of its field

1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed, 4 citations in OpenAlex.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 2 institutions in 1 country.

Zhe WangCollege of Food Engineering, Harbin University of Commerce, Harbin 150076, China.ORCID 0009-0007-0179-2440

Guanlong LiKey Laboratory of Corn Deep Processing Theory and Technology of Heilongjiang Province, College of Food and Bioengineering, Qiqihar University, Qiqihar 161006, China.

Xiaolan LiuCollege of Food Engineering, Harbin University of Commerce, Harbin 150076, China.

Qiqihar University · CNHarbin University of Commerce · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Alcohol dehydrogenase (ADH) plays a pivotal role in constraining alcohol metabolism. Assessing the ADH-activating activity in vitro can provide insight into the capacity to accelerate ethanol metabolism in vivo. In this study, ADH-activating peptides were prepared from corn protein meal (CGM) using enzymatic hydrolysis, and these peptides were subsequently identified following simulated gastrointestinal digestion and their absorption through the Caco-2 cell monolayer membrane. The current investigation revealed that corn protein hydrolysate hydrolyzed using alcalase exhibited the highest ADH activation capability, maintaining an ADH activation rate of 52.93 ± 2.07% following simulated gastrointestinal digestion in vitro. After absorption through the Caco-2 cell monolayer membrane, ADH-activating peptides were identified. Among them, SSNCQPF, TGCPVLQ, and QPQQPW were validated to possess strong ADH activation activity, with EC

Indexed as

Alcohol DehydrogenaseZea maysCaco-2 CellsHumansMolecular Docking SimulationPeptidesProtein HydrolysatesAlcohol DehydrogenasePeptidesProtein HydrolysatesADH activating peptidesCaco-2 cell monolayercorngastrointestinal digestionidentification

Identifiers

PMID38611803

DOI10.3390/molecules29071523

PMCPMC11013139

OpenAlexW4393279043

What OpenQuestion holds

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LicenceCC BY

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Registered trials

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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.