Evidence map›Paper›PMID 40394587›Full record

ArticleMicrobial cell factories2025

Comparative analysis of pre-treatment strategies and bacterial strain efficiency for improvement of feather hydrolysis.

Clémentine Isembart, Boris Zimmermann, Josipa Matić, Cristian Bolaño Losada, Nils K Afseth, Achim Kohler, Svein J Horn, Vincent Eijsink, Piotr Chylenski, Volha Shapaval

Abstract readComparative Study
In one paragraph

Article in Microbial cell factories, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. Proteolytic and non-proteolytic mechanisms of keratin degradation inApplied and environmental microbiology · 2025
    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.

Clémentine IsembartFaculty of Science and Technology, Norwegian University of Life Sciences, Drøbakveien 31, Ås, 1432, Norway. clementine.isembart@nmbu.no.
Boris ZimmermannFaculty of Science and Technology, Norwegian University of Life Sciences, Drøbakveien 31, Ås, 1432, Norway.
Josipa MatićNofima AS, Ås, 1432, Norway.
Cristian Bolaño LosadaFaculty of Science and Technology, Norwegian University of Life Sciences, Drøbakveien 31, Ås, 1432, Norway.
Nils K AfsethNofima AS, Ås, 1432, Norway.
Achim KohlerFaculty of Science and Technology, Norwegian University of Life Sciences, Drøbakveien 31, Ås, 1432, Norway.
Svein J HornFaculty of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences, Ås, 1432, Norway.
Vincent EijsinkFaculty of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences, Ås, 1432, Norway.
Piotr ChylenskiNorilia AS, Oslo, 0513, Norway.
Volha ShapavalFaculty of Science and Technology, Norwegian University of Life Sciences, Drøbakveien 31, Ås, 1432, Norway.

Funding

BYPROVALUE 301834Norwegian Fund for Research Fees for Agricultural Products 354160SFI Industrial Biotechnology 301834
6 · The paper itself

Abstract

backgroundFeathers are a major by-product of the poultry industry, which poses an environmental challenge due to the recalcitrant structure of keratin, making them resistant to degradation. Traditional methods of feather handling, like conversion to feather meal, are energy-intensive and have limited efficiency. Biotechnological approaches, particularly microbial hydrolysis, offer a novel and more sustainable alternative for keratin degradation. This study evaluated feather hydrolysis by two bacterial strains, newly characterized cold-adapted Arthrobacter oryzae (BIM B-1663) and Bacillus licheniformis (CCM 2145

resultsBoth bacterial strains were able to degrade pretreated feathers with a degradation efficiency of 75 to 90%, resulting in high ratios of nitrogen to carbon in the hydrolysates. B. licheniformis confirmed its enzymatic capabilities with high levels of general and specific protease activity and furthermore presented enriched amounts of amino acids of industrial interest. A. oryzae showed a much higher keratinase/protease activity ratio, demonstrating high specificity and efficiency of its enzymes. Autoclaving emerged as the most important determinant of microbial degradation efficiency and influenced the composition (peptide pattern, amino acid content, and chemical composition assessed through FTIR) of the resulting hydrolysates. Feather drying, although not improving microbial degradation efficiencies, had a considerable impact on hydrolysate composition.

conclusionsThe results show that both tested bacterial strains can efficiently degrade autoclaved feathers but use distinct enzymatic strategies to do so. Enriched profiles in amino acids and high nitrogen content in the hydrolysates also advocate for the benefits of microbial feather hydrolysis over an enzymatic one. To the authors' knowledge this study is the first to report a comprehensive evaluation of the impact of various feather pre-treatment methods on the efficiency of subsequent microbial feather hydrolysis and is the first one to report enrichment in phenylalanine, lysine, and tyrosine secreted by B. licheniformis.

Indexed as

ArthrobacterBacillus licheniformisFeathersAnimalsChickensHydrolysisKeratinsPeptide HydrolaseskeratinaseKeratinsPeptide Hydrolases

Identifiers

PMID40394587
PMCPMC12093666

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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.