Evidence map›Paper›PMID 32572051›Full record

ArticleScientific reports2020

Novel keratinolytic enzymes, discovered from a talented and efficient bacterial keratin degrader.

Yuhong Huang, Mateusz Łężyk, Florian-Alexander Herbst, Peter Kamp Busk, Lene Lange

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
3.1field-weighted citation impact, top 8% of its field
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

10 citing papers in PubMed, 32 citations in OpenAlex.

  1. Proteolytic and non-proteolytic mechanisms of keratin degradation inApplied and environmental microbiology · 2025
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  5. Characterization of high-yield Bacillus subtilis cysteine protease for diverse industrial applications.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2023
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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

5 authors at 3 institutions in 2 countries.

Yuhong HuangDepartment of Biotechnology and Biomedicine, Technical University of Denmark, Building 224, Søltofts Plads, 2800, Kongens Lyngby, Denmark.
Mateusz ŁężykDepartment of Biotechnology and Biomedicine, Technical University of Denmark, Building 224, Søltofts Plads, 2800, Kongens Lyngby, Denmark.
Florian-Alexander HerbstCenter for Microbial Communities, Department of Chemistry and Bioscience, Aalborg University, Fredrik Bajers Vej 7H, 9220, Aalborg East, Denmark.
Peter Kamp BuskDepartment of Biotechnology and Biomedicine, Technical University of Denmark, Building 224, Søltofts Plads, 2800, Kongens Lyngby, Denmark.
Lene LangeDepartment of Biotechnology and Biomedicine, Technical University of Denmark, Building 224, Søltofts Plads, 2800, Kongens Lyngby, Denmark. lene.lange2@gmail.com.
Technical University of Denmark · DKAalborg University · DKRoskilde University · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Huge quantities of keratinaceous waste are a substantial and almost totally unexploited protein resource which could be upgraded for use as high value-added products by efficient keratinolytic enzymes. In this study, we found that Bacillus sp. 8A6 can efficiently degrade chicken feather after 24 h growth. According to phylogenetic analysis, the strain (formerly identified as Bacillus pumilus 8A6) belongs to the B. pumilus species clade but it is more closely related to B. safensis. Hotpep predicted 233 putative proteases from Bacillus sp. 8A6 genome. Proteomic analysis of culture broths from Bacillus sp. 8A6 cultured on chicken feathers or on a mixture of bristles and hooves showed high abundance of proteins with functions related to peptidase activity. Five proteases (one from family M12, one from family S01A, two from family S08A and one from family T3) and four oligopeptide and dipeptide binding proteins were highly expressed when Bacillus sp. 8A6 was grown in keratin media compared to LB medium. This study is the first to report that bacterial proteases in families M12, S01A and T3 are involved in keratin degradation together with proteases from family S08.

Indexed as

AnimalsBacillusBacillus pumilusChickensCysteine ProteasesFeathersKeratinsMetalloproteasesPeptide HydrolasesPhylogenyProteomicsSerine ProteasesCysteine ProteasesKeratinsMetalloproteasesPeptide HydrolasesSerine Proteases

Identifiers

PMID32572051
PMCPMC7308268
OpenAlexW3036988308

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.