Evidence map›Paper›PMID 39569156›Full record

ArticleACS catalysis2024

Selective Hydrolysis of Heterooligosaccharides by Poly(acrylate) Gel Catalysts.

Susanne Striegler

Abstract read
In one paragraph

Article in ACS catalysis, 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
–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

1 author.

Susanne StrieglerDepartment of Chemistry and Biochemistry, University of Arkansas, 345 North Campus Walk, Fayetteville, Arkansas 72701, United States.ORCID https://orcid.org/0000-0002-2233-3784

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Natural glycoside hydrolases are distinguished by their ability to hydrolyze glycosidic bonds with high efficiency and selectivity. This feature is achieved through specific interactions in the active site during catalytic turnover and is not just facilitated by two catalytically active amino acids. Intrigued by these features, a biomimetic α-galactosidase mimic was developed using an empirical catalyst design. Starting with a library of 704 gels of which 250 have a unique composition synthesized from TEGDMA cross-linker and 7 selected monomers, 238 monomodal gels are evaluated for their ability to hydrolyze the 1→6 α-glycosidic bond in the disaccharide melibiose. Among those, 13 polyacrylate gels with the potential for high catalytic activity are identified using spectrophotometric screening assays based on Schiff bases formed with toluidine. The best-performing polyacrylate (gel A) was found to have a 1500-fold higher proficiency to hydrolyze the 1→6 α-glycosidic bond in melibiose over the 1→2 α-glycosidic bond in sucrose, translating to selective hydrolysis of the glycosidic linkages in the trisaccharide raffinose. The matrix of gel A is composed of 25 mol % TEGDMA cross-linker and equimolar amounts of cyclohexyl, butyl, and benzyl acrylate accounting for CH-π and hydrophobic interaction in the surrounding of a hydrolytic binuclear Cu(II) complex. The combined observations underline a paramount influence of matrix-stabilizing effects on the transition state of the hydrolysis of glycosidic bonds and may pave the way for the rapid development of catalysts transforming biomass.

Identifiers

PMID39569156
PMCPMC11574753

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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.