Evidence map›Paper›PMID 41520026›Full record

ArticleApplied microbiology and biotechnology2026

Unlocking the Zn-enriching potential of industrial yeast strains-an experimental journey from metal analysis to proteomics.

Gina Grimmer, Julia Muenzner, Maximillian Schmacht, Maria Angels Subirana, Iris H Valido, Philip Nickl, Paul M Dietrich, Ievgen S Donskyi, Dirk Schaumlöffel, Martin Hageböck and 6 more

Abstract read
In one paragraph

Article in Applied microbiology and biotechnology, 2026. 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

16 authors.

Gina Grimmer *Department of Food Chemistry, Institute of Nutritional Science, University of Potsdam, Arthur-Scheunert-Allee 114-116, 14558, Nuthetal, Germany.
Julia Muenzner *Department of Biochemistry, Charité Universitätsmedizin Berlin, 10117, Berlin, Germany.
Maximillian SchmachtDepartment Bioprocess Engineering and Applied Microbiology, Versuchs- und Lehranstalt für Brauerei in Berlin (VLB) e.V, Seestraße 13, 13353, Berlin, Germany.
Maria Angels SubiranaCNRS, Université de Pau et des Pays de l'Adour, Institut des Sciences Analytiques et de Physico-Chimie pour l'Environnement et les Matériaux (IPREM) UMR 5254, Université de Pau et des Pays de l'Adour, Hélioparc, 2 avenue Pierre Angot, 64053, Pau, France.
Iris H ValidoCNRS, Université de Pau et des Pays de l'Adour, Institut des Sciences Analytiques et de Physico-Chimie pour l'Environnement et les Matériaux (IPREM) UMR 5254, Université de Pau et des Pays de l'Adour, Hélioparc, 2 avenue Pierre Angot, 64053, Pau, France.
Philip NicklInstitut für Chemie und Biochemie, Freie Universität Berlin, Takustr. 3, 14195, Berlin, Germany.
Paul M DietrichSPECS Surface Nano Analysis GmbH, Voltastrasse 5, 13355, Berlin, Germany.
Ievgen S DonskyiInstitut für Chemie und Biochemie, Freie Universität Berlin, Takustr. 3, 14195, Berlin, Germany.
Dirk SchaumlöffelCNRS, Université de Pau et des Pays de l'Adour, Institut des Sciences Analytiques et de Physico-Chimie pour l'Environnement et les Matériaux (IPREM) UMR 5254, Université de Pau et des Pays de l'Adour, Hélioparc, 2 avenue Pierre Angot, 64053, Pau, France.
Martin HageböckDepartment Bioprocess Engineering and Applied Microbiology, Versuchs- und Lehranstalt für Brauerei in Berlin (VLB) e.V, Seestraße 13, 13353, Berlin, Germany.
Michael MüllederCore Facility - High Throughput Mass Spectrometry, Charité Universitätsmedizin Berlin, Berlin, Germany.
Markus RalserDepartment of Biochemistry, Charité Universitätsmedizin Berlin, 10117, Berlin, Germany.
Hajo HaaseDepartment of Food Chemistry and Toxicology, Institute of Food Technology and Food Chemistry, Technische Universität Berlin, Straße des 17. Juni 135, 10623, Berlin, Germany.
Martin SenzDepartment Bioprocess Engineering and Applied Microbiology, Versuchs- und Lehranstalt für Brauerei in Berlin (VLB) e.V, Seestraße 13, 13353, Berlin, Germany.
Maria MaaresDepartment of Food Chemistry, Institute of Nutritional Science, University of Potsdam, Arthur-Scheunert-Allee 114-116, 14558, Nuthetal, Germany. maria.maares.1@uni-potsdam.de.
Claudia KeilDepartment of Food Chemistry and Toxicology, Institute of Food Technology and Food Chemistry, Technische Universität Berlin, Straße des 17. Juni 135, 10623, Berlin, Germany. c.keil@tu-berlin.de.

Funding

Deutsche Forschungsgemeinschaft grant 492697668Germany's Excellence Strategy EXC 3118/1 - project number 533770413PHC PROCOPE 50838WJ/57702758
6 · The paper itself

Abstract

Nutritional supplements such as trace element-enriched yeasts are becoming increasingly popular to overcome the worldwide problem of zinc (Zn) deficiency. Unlike selenium-enriched yeast, which is already authorized in the European Union, Zn-enriched yeasts (ZnY) have not yet been approved for food purposes in the European Union, as their evaluation is still ongoing, demanding more comprehensive data regarding the Zn species present in ZnY. This study screens ten different industrial yeast strains regarding their Zn-enrichment quota, with further characterization of selected strains using spectroscopic and proteomic approaches. Microfermentation experiments on the industrial yeasts showed Zn levels spanning 0.06-51 pg/cell. Large-scale fermentation in bioreactors was carried out with two strains excelling in either biomass or Zn accumulation. A combination of inductively coupled plasma mass spectrometry (ICP-MS) and various spectroscopic methods confirmed the Zn enrichment, while suggesting that fractions of the Zn accumulated on the cell surface, with simultaneously high values of phosphorus being present. Speciation via X-ray absorption spectroscopy (XAS) analyses revealed that Zn species are transformed and Zn is coordinated to P-O-ligands and to amino acid ligands in both strains. Proteomic analysis showed that ZnY cells moved from a Zap1-governed Zn balance to an intracellular excess response, implying cellular Zn uptake. This study demonstrates that, in a Zn-excess medium, industrial yeast strains exhibit variability in Zn-accumulation capacity, cellular Zn-localization, and regulatory responses involving the expression of Zn-binding proteins. The presented findings contribute to optimizing industrial fermentation processes for producing Zn-rich yeast biomass and enhance the understanding of Zn regulation in yeast, aiding in the approval of Zn-enriched yeasts for supplements and novel food applications. KEY POINTS: • Zn enrichment in yeasts is strongly time and strain dependent • Zn proteome changes under Zn excess suggest that Zn is partly internalized in the yeast cells • Beside proteins, phosphorous compounds seem to be Zn-binding ligands in Zn-enriched yeast.

Indexed as

Saccharomyces cerevisiaeYeastsZincBiomassBioreactorsFermentationIndustrial MicrobiologyMass SpectrometryMetalsProteomeProteomicsTrace ElementsX-Ray Absorption SpectroscopyMetalsProteomeTrace ElementsZincProteomicsXASZinc-enriched yeastZinc speciationZinc supplement

Identifiers

PMID41520026
PMCPMC12791086

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.