Evidence map›Paper›PMID 41353650›Full record

ArticleJournal of agricultural and food chemistry2025

Comparative Characterization of Oxidative Enzymes for Arabinoxylan and Protein Cross-Linking via Ferulic Acid and Tyrosine in Model Systems.

Katharina Hoefler, Ulrich Sukop, Elisabeth Reiter, Denisse Bender, Mario Jekle, Patrik Roch, Margit Cichna-Markl, Stefano D'Amico, Regine Schoenlechner

Abstract readComparative Study
PubMed Full text at PMC Publisher
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. 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

9 authors.

Katharina HoeflerInstitute for Animal Nutrition and Feed, AGES - Austrian Agency for Health and Food Safety, Spargelfeldstraße 191, 1220 Vienna, Austria.
Ulrich SukopDepartment of Biotechnology and Food Science, BOKU University, Muthgasse 18, 1190 Vienna, Austria.
Elisabeth ReiterInstitute for Animal Nutrition and Feed, AGES - Austrian Agency for Health and Food Safety, Spargelfeldstraße 191, 1220 Vienna, Austria.
Denisse BenderDepartment of Biotechnology and Food Science, BOKU University, Muthgasse 18, 1190 Vienna, Austria.
Mario JekleDepartment of Plant-based Foods, University of Hohenheim, Garbenstraße 25, 70599 Stuttgart, Germany.
Patrik RochInstitute for Animal Nutrition and Feed, AGES - Austrian Agency for Health and Food Safety, Spargelfeldstraße 191, 1220 Vienna, Austria.
Margit Cichna-MarklDepartment of Analytical Chemistry, University of Vienna - Faculty of Chemistry, Währinger Straße 38, 1090 Vienna, Austria.ORCID 0000-0001-8699-674X
Stefano D'AmicoInstitute for Animal Nutrition and Feed, AGES - Austrian Agency for Health and Food Safety, Spargelfeldstraße 191, 1220 Vienna, Austria.ORCID 0000-0002-6702-7158
Regine SchoenlechnerDepartment of Biotechnology and Food Science, BOKU University, Muthgasse 18, 1190 Vienna, Austria.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

This study comparatively investigated various oxidoreductases (laccase, peroxidase, tyrosinase, and glucose oxidase) and their combinations for their conversion capability of available connection points, tyrosine in proteins and ferulic acid (FA) in arabinoxylans, as useful cross-linking tools. Therefore, substrate specificity and pH- and temperature-dependent activity were studied in different substrate ratios. Enzyme characteristics varied notably across standard assays, where even substrate-dependent shifts in pH optima occurred. Combining enzymes significantly reduced the

Indexed as

Coumaric AcidsOxidoreductasesTyrosineXylansGlucose OxidaseHydrogen-Ion ConcentrationKineticsLaccaseMonophenol MonooxygenaseOxidation-ReductionPeroxidaseSubstrate SpecificityarabinoxylanCoumaric Acidsferulic acidGlucose OxidaseLaccaseMonophenol MonooxygenaseOxidoreductasesPeroxidaseTyrosineXylansbiocatalysisbiopolymer engineeringbuffer compatibilityoxidative couplingphenolic compounds

Identifiers

PMID41353650
PMCPMC12715794

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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.