Evidence map›Paper›PMID 40741084›Full record

ArticleFood chemistry. Molecular sciences2025

Enhanced catalytic activity of a novel trypsin by semi-rational design with mechanistic insights from molecular simulations.

Jia Chen, Guangyang Jiang, Yongqiang Tian

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Food chemistry. Molecular sciences, 2025. 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

3 authors.

Jia ChenCollege of Biomass Science and Engineering, Sichuan University, Chengdu, China.
Guangyang JiangCollege of Biomass Science and Engineering, Sichuan University, Chengdu, China.
Yongqiang TianCollege of Biomass Science and Engineering, Sichuan University, Chengdu, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Trypsin is widely used in the food industry for meat processing, dairy production and seafood treatment. However, the industrial application of trypsin is constrained by the pathogenic risks associated with animal-derived trypsin and the low enzymatic activity of microbial-derived trypsin. This study aimed to enhance the catalytic activity of a novel trypsin heterologously expressed in

Indexed as

Bacillus subtilisCatalytic efficiencyIndustrial enzymesMolecular dynamics simulationsSemi-rational designTrypsin engineering

Identifiers

PMID40741084
PMCPMC12309265

What OpenQuestion holds

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Registered trials

None linked

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.