Evidence mapPaperPMID 41897756Full record

ArticleFoods (Basel, Switzerland)2026

Protease Selection Influences Molecular Weight, In Vitro Antioxidant Activity and LO2 Cellular Protective Effects of Oyster Protein Hydrolysates.

Can Huang, Lu Li, Ruifang Wang, Guohong Wu, Hejian Xiong, Ying Ma

Abstract read
In one paragraph

Article in Foods (Basel, Switzerland), 2026. 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
field-weighted citation impact
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.

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

6 authors.

Can HuangCollege of Ocean Food and Biological Engineering, Jimei University, Xiamen 361021, China.ORCID 0009-0007-4451-5232
Lu LiCollege of Ocean Food and Biological Engineering, Jimei University, Xiamen 361021, China.
Ruifang WangCollege of Ocean Food and Biological Engineering, Jimei University, Xiamen 361021, China.
Guohong WuCollege of Ocean Food and Biological Engineering, Jimei University, Xiamen 361021, China.
Hejian XiongCollege of Ocean Food and Biological Engineering, Jimei University, Xiamen 361021, China.
Ying MaFisheries College, Jimei University, Xiamen 361021, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

This study compared the effectiveness of alkaline protease, neutral protease, trypsin, and papain in hydrolyzing oyster proteins and evaluated the antioxidant activities of the resulting hydrolysates. Alkaline protease achieved the highest degree of hydrolysis (30.96%) and the highest proportion of peptides ≤1 kDa (64.23%). Papain showed the lowest hydrolysis degree (18.29%). After separation by Sephadex G-15 gel filtration chromatography, the resulting low-molecular-weight peptide fractions (≤1 kDa) from each hydrolysate exhibited higher in vitro antioxidant activity than the higher-molecular-weight fractions (>1 kDa). Notably, trypsin and papain-derived low-molecular-weight fractions (OPP-T2 and OPP-P2) demonstrated stronger DPPH radical scavenging and inhibition of linoleic acid autoxidation than those from alkaline and neutral proteases. Cell experiments revealed that all low-molecular-weight fractions effectively alleviated H

Indexed as

cellular antioxidant activityDPPH radical scavenginglinoleic acid autoxidation inhibitionmolecular weightoyster peptide

Identifiers

PMID41897756
PMCPMC13024773

What Socratic holds

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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 Socratic graph.