Evidence map›Paper›PMID 39797788›Full record

ArticleJournal of agricultural and food chemistry2025

Identification and Characterization of a New Thermophilic κ-Carrageenan Sulfatase.

Nanna Rhein-Knudsen, Diego S Reyes-Weiss, Leesa J Klau, Alexandra Jeudy, Thomas Roret, Runar Stokke, Vincent G H Eijsink, Finn L Aachmann, Mirjam Czjzek, Svein Jarle Horn

Abstract read
In one paragraph

Article in Journal of agricultural and food chemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

10 authors.

Nanna Rhein-KnudsenFaculty of Chemistry, Biotechnology, and Food Science, NMBU Norwegian University of Life Sciences, P.O. Box 5003, 1432 Aas, Norway.ORCID 0000-0001-6695-346X
Diego S Reyes-WeissFaculty of Chemistry, Biotechnology, and Food Science, NMBU Norwegian University of Life Sciences, P.O. Box 5003, 1432 Aas, Norway.
Leesa J KlauDepartment of Biotechnology and Food Science, NTNU Norwegian University of Science and Technology, Sem Sælands vei 6/8, 7419 Trondheim, Norway.
Alexandra JeudyCNRS, Integrative Biology of Marine Models, Station Biologique de Roscoff, Sorbonne Universitée, 29680 Roscoff, France.
Thomas RoretCNRS, Integrative Biology of Marine Models, Station Biologique de Roscoff, Sorbonne Universitée, 29680 Roscoff, France.
Runar StokkeDepartment of Biological Sciences and Centre for Deep Sea Research, University of Bergen, 5020 Bergen, Norway.
Vincent G H EijsinkFaculty of Chemistry, Biotechnology, and Food Science, NMBU Norwegian University of Life Sciences, P.O. Box 5003, 1432 Aas, Norway.ORCID 0000-0002-9220-8743
Finn L AachmannDepartment of Biotechnology and Food Science, NTNU Norwegian University of Science and Technology, Sem Sælands vei 6/8, 7419 Trondheim, Norway.ORCID 0000-0003-1613-4663
Mirjam CzjzekCNRS, Integrative Biology of Marine Models, Station Biologique de Roscoff, Sorbonne Universitée, 29680 Roscoff, France.
Svein Jarle HornFaculty of Chemistry, Biotechnology, and Food Science, NMBU Norwegian University of Life Sciences, P.O. Box 5003, 1432 Aas, Norway.ORCID 0000-0002-1590-9001

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Carrageenans are sulfated polysaccharides found in the cell wall of certain red seaweeds. They are widely used in the food industry for their gelling and stabilizing properties. In nature, carrageenans undergo enzymatic modification and degradation by marine organisms. Characterizing these enzymes is crucial for understanding carrageenan utilization and may eventually enable the development of targeted processes to modify carrageenans for industrial applications. In our study, we characterized a κ-carrageenan sulfatase, AMOR_S1_16A, belonging to the sulfatase S1_16 subfamily, which selectively desulfates the nonreducing end galactoses of κ-carrageenan oligomers in an exomode. Notably, AMOR_S1_16A represents the first κ-carrageenan sulfatase within the S1_16 subfamily and exhibits a novel enzymatic activity. This study provides further understanding of the substrate specificity and characteristics of the S1_16 subfamily. Moreover, this research highlights that many processes and enzymes remain to be discovered to fully understand carrageenan utilization pathways and to develop enzymatic processes for carrageenan modification and processing.

Indexed as

Bacterial ProteinsCarrageenanSulfatasesEnzyme StabilityRhodophytaSubstrate SpecificityBacterial ProteinsCarrageenanSulfatases4-O-sulfatasecarbohydrate sulfatasecarrageenan modificationsubstrate specificitysulfated carbohydrate

Identifiers

PMID39797788
PMCPMC11760155

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.