Evidence map›Paper›PMID 32580707›Full record

ArticleMicrobial cell factories2020

An alternative for proteinase K-heat-sensitive protease from fungus Onygena corvina for biotechnology: cloning, engineering, expression, characterization and special application for protein sequencing.

Piotr M Skowron, Daria Krefft, Robert Brodzik, Paulina Kasperkiewicz, Marcin Drag, Klaus-Peter Koller

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Microbial cell factories, 2020. 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
0.9field-weighted citation impact, top 28% 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

2 citing papers in PubMed, 11 citations in OpenAlex.

  1. Proteolytic and non-proteolytic mechanisms of keratin degradation inApplied and environmental microbiology · 2025
    Article
  2. Microbial proteases and their applications.Frontiers in microbiology · 2023
    Review
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

6 authors at 4 institutions in 2 countries.

Piotr M SkowronDepartment of Molecular Biotechnology, Faculty of Chemistry, University of Gdansk, Wita Stwosza 63 Street, 80-308, Gdansk, Poland. piotr.skowron@ug.edu.pl.ORCID http://orcid.org/0000-0003-1345-3271
Daria KrefftDepartment of Molecular Biotechnology, Faculty of Chemistry, University of Gdansk, Wita Stwosza 63 Street, 80-308, Gdansk, Poland.
Robert BrodzikBLIRT S.A., Trzy Lipy 3/1.38 Street, 80-172, Gdansk, Poland.
Paulina KasperkiewiczDepartment of Chemical Biology and Bioimaging, Wroclaw University of Science and Technology, Wyb. Wyspianskiego 27 Street, 50-370, Wroclaw, Poland.
Marcin DragDepartment of Chemical Biology and Bioimaging, Wroclaw University of Science and Technology, Wyb. Wyspianskiego 27 Street, 50-370, Wroclaw, Poland.
Klaus-Peter KollerInstitute for Molecular Bio Science, University Frankfurt, Max-von-Laue-Str. 9, 60438, Frankfurt, Germany.
University of Gdańsk · PLWrocław University of Science and Technology · PLBioLab Innovative Research Technologies (Poland) · PLGoethe University Frankfurt · DE

Funding

Barentzymes AS, Norway company funds
6 · The paper itself

Abstract

backgroundA neutral, heat-sensitive serine protease (NHSSP) originating from the feather-degrading fungus Onygena corvina (O. corvina) was described and defined as an alkaline serine protease of the subtilisin type S8 family, exhibiting an enzymatic activity at neutral pH. Generally, broad specificity proteases, such as proteinase K or trypsin, have found numerous applications in research and biotechnology.

resultsWe report the cloning and expression in the yeast PichiaPink™ system, as well as purification, and characterization of the NHSSP. Recombinant, His

conclusionsThe NHSSP was produced as a recombinant protein with high efficiency. Compared to proteinase K, the most common serine protease used, NHSSP shows an approx. twofold higher specific activity. Protein sequencing can be a valuable technical application for the protease. The protein coverage is significantly higher in comparison to trypsin and reaches about 84-100% for β-lactoglobulin (BLG), antibody (mAb) light and heavy chains. Furthermore, the option to perform digestions at neutral to slightly acidic pH-values down to pH 5.0 avoids modification of peptides, e.g. due to deamidation.

Indexed as

Fungal ProteinsSerine ProteasesEnzyme StabilityHot TemperatureHydrogen-Ion ConcentrationIndustrial MicrobiologyKineticsOnygenalesProtein Processing, Post-TranslationalRecombinant ProteinsFungal ProteinsRecombinant ProteinsSerine ProteasesExpressionFood processingOnygena corvinaPichia pastorisProteaseProteinase KProtein degradationProtein sequencingSerine proteaseWaste processing

Identifiers

PMID32580707
PMCPMC7313183
OpenAlexW3037296074

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.