Evidence map›Paper›PMID 36912209›Full record

ArticleEssays in biochemistry2023

Carbohydrate esterases involved in deacetylation of food components by the human gut microbiota.

Sabina Leanti La Rosa, Lars J Lindstad, Bjørge Westereng

Open access · hybridAbstract read
In one paragraph

Article in Essays in biochemistry, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
2.1field-weighted citation impact, top 14% 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

7 citing papers in PubMed, 13 citations in OpenAlex.

  1. Mechanisms ofAnimal nutrition (Zhongguo xu mu shou yi xue hui) · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Genetic analysis of a β-1,3/1,4-glucan utilization gene cluster inBioscience of microbiota, food and health · 2025
    Article
  6. Review
  7. Article
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 1 institution in 1 country.

Sabina Leanti La RosaFaculty of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences, 1433, Aas, Norway.ORCID 0000-0003-3527-8101
Lars J LindstadFaculty of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences, 1433, Aas, Norway.ORCID 0000-0003-2146-7817
Bjørge WesterengFaculty of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences, 1433, Aas, Norway.ORCID 0000-0002-5141-7231
Norwegian University of Life Sciences · NO

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Non-carbohydrate modifications such as acetylations are widespread in food stuffs as well as they play important roles in diverse biological processes. These modifications meet the gut environment and are removed from their carbohydrate substrates by the resident microbiota. Among the most abundant modifications are O-acetylations, contributing to polysaccharides physico-chemical properties such as viscosity and gelling ability, as well as reducing accessibility for glycosyl hydrolases, and thus hindering polysaccharide degradation. Of particular note, O-acetylations increase the overall complexity of a polymer, thus requiring a more advanced degrading machinery for microbes to utilize it. This minireview describes acetylesterases from the gut microbiota that deacetylate various food polysaccharides, either as natural components of food, ingredients, stabilizers of microbial origin, or as part of microbes for food and beverage preparations. These enzymes include members belonging to at least 8 families in the CAZy database, as well as a large number of biochemically characterized esterases that have not been classified yet. Despite different structural folds, most of these acetylesterases have a common acid-base mechanism and belong to the SGNH hydrolase superfamily. We highlight examples of acetylesterases that are highly specific to one substrate and to the position of the acetyl group on the glycosyl residue of the carbohydrate, while other members that have more broad substrate specificity. Current research aimed at unveiling the functions and regioselectivity of acetylesterases will help providing fundamental mechanistic understanding on how dietary components are utilized in the human gut and will aid developing applications of these enzymes to manufacture novel industrial products.

Indexed as

EsterasesGastrointestinal MicrobiomeHumansPolysaccharidesEsterasesPolysaccharidescarbohydrate metabolismdeacetylationenzymologystructural biology

Identifiers

PMID36912209
PMCPMC10154613
OpenAlexW4324017824

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390

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.