Evidence map›Paper›PMID 40149951›Full record

ArticleBiomolecules2025

Cold-Active Starch-Degrading Enzymes from a Cold and Alkaline Greenland Environment: Role of Ca

Malthe Kjær Bendtsen, Jan Stanislaw Nowak, Pedro Paiva, Marcos López Hernández, Pedro Ferreira, Jan Skov Pedersen, Nicolai Sundgaard Bekker, Elia Viezzi, Francesco Bisiak, Ditlev E Brodersen and 7 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biomolecules, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Article
  3. 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

17 authors.

Malthe Kjær BendtsenInterdisciplinary Nanoscience Center, Gustav Wieds Vej 14, 8000 Aarhus, Denmark.ORCID 0009-0002-8505-9994
Jan Stanislaw NowakInterdisciplinary Nanoscience Center, Gustav Wieds Vej 14, 8000 Aarhus, Denmark.
Pedro PaivaLAQV, REQUIMTE, Departamento de Química e Bioquímica, Faculdade de Ciências Universidade do Porto, Rua do Campo Alegre, s/n, 4169-007 Porto, Portugal.ORCID 0000-0002-7003-6055
Marcos López HernándezInterdisciplinary Nanoscience Center, Gustav Wieds Vej 14, 8000 Aarhus, Denmark.ORCID 0000-0001-7843-7374
Pedro FerreiraLAQV, REQUIMTE, Departamento de Química e Bioquímica, Faculdade de Ciências Universidade do Porto, Rua do Campo Alegre, s/n, 4169-007 Porto, Portugal.ORCID 0000-0001-7015-5460
Jan Skov PedersenInterdisciplinary Nanoscience Center, Gustav Wieds Vej 14, 8000 Aarhus, Denmark.
Nicolai Sundgaard BekkerDepartment of Chemistry and Bioscience, Aalborg University, Fredrik Bajers Vej 7H, 9220 Aalborg, Denmark.
Elia ViezziInterdisciplinary Nanoscience Center, Gustav Wieds Vej 14, 8000 Aarhus, Denmark.
Francesco BisiakDepartment of Molecular Biology and Genetics, Aarhus University, Universitetsbyen 81, 8000 Aarhus, Denmark.ORCID 0000-0001-5375-6264
Ditlev E BrodersenDepartment of Molecular Biology and Genetics, Aarhus University, Universitetsbyen 81, 8000 Aarhus, Denmark.ORCID 0000-0002-5413-4667
Lars Haastrup PedersenDepartment of Chemistry and Bioscience, Aalborg University, Fredrik Bajers Vej 7H, 9220 Aalborg, Denmark.
Athanasios ZervasDepartment of Environmental Science, Aarhus University, 4000 Roskilde, Denmark.ORCID 0000-0002-4706-4023
Pedro A FernandesLAQV, REQUIMTE, Departamento de Química e Bioquímica, Faculdade de Ciências Universidade do Porto, Rua do Campo Alegre, s/n, 4169-007 Porto, Portugal.ORCID 0000-0003-2748-4722
Maria Joao RamosLAQV, REQUIMTE, Departamento de Química e Bioquímica, Faculdade de Ciências Universidade do Porto, Rua do Campo Alegre, s/n, 4169-007 Porto, Portugal.
Peter StougaardDepartment of Environmental Science, Aarhus University, 4000 Roskilde, Denmark.
Mariane Schmidt ThøgersenDepartment of Environmental Science, Aarhus University, 4000 Roskilde, Denmark.ORCID 0000-0003-0799-6894
Daniel E OtzenInterdisciplinary Nanoscience Center, Gustav Wieds Vej 14, 8000 Aarhus, Denmark.ORCID 0000-0002-2918-8989

Funding

COMPUTER AIDED ANALYSIS OF ELECTROCARDIOGRAPHYZ01CT000002 · CIT · COMPUTER RESEARCH AND TECHNOLOGY · PI BAILEY, JAMES J. · 1985 to 2003
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Danmarks Frie Forskningsfond 0217-00052BDanmarks Frie Forskningsfond 9041-00123BFundação para a Ciência e Tecnologia CEECINST/00136/2021/CP2820/CT0002Fundação para a Ciência e Tecnologia LA/P/0008/2020Fundação para a Ciência e Tecnologia UIDB/50006/2020Fundação para a Ciência e Tecnologia UIDP/50006/2020Intramural NIH HHS Z01 CT000002Novo Nordisk Foundation NNF22OC0072891
6 · The paper itself

Abstract

Cold-active enzymes hold promise for energy-efficient processes. Amylases are widely used in household and industrial applications, but only a few are cold-active. Here we describe three novel secreted amylases, Rho13, Ika2 and I3C6, all from bacteria growing in the cold and alkaline ikaite columns in Greenland. They all hydrolyzed starch to smaller malto-oligomers, but only Rho13 and Ika2 hydrolyzed cyclodextrins, and only Ika2 displayed transglycosylation activity. Ika2 forms a stable dimer, while both Rho13 and I3C6 are mainly monomeric. They all have optimal active temperatures around 30-35 °C and significant enzymatic activity below 20 °C, but Rho13 and I3C6 had an alkaline optimal pH, while Ika2 was markedly acidophilic. They showed complex dependence on Ca

Indexed as

Bacterial ProteinsCalciumStarchCold TemperatureEnzyme StabilityGreenlandHydrogen-Ion ConcentrationMolecular Dynamics SimulationBacterial ProteinsCalciumStarchmolecular dynamicsprotein stabilitypsychrophilic enzymes

Identifiers

PMID40149951
PMCPMC11940188

What OpenQuestion 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 OpenQuestion graph.