Evidence map›Paper›PMID 32852125›Full record

ArticleMicrobiologyOpen2020

Recombinant expression of an l-amino acid oxidase from the fungus Hebeloma cylindrosporum in Pichia pastoris including fermentation.

Marc Christian Heß, Svenja Bloess, Joe Max Risse, Karl Friehs, Gabriele Fischer von Mollard

Open access · goldAbstract read
In one paragraph

Article in MicrobiologyOpen, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.6field-weighted citation impact, top 34% 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

6 citing papers in PubMed, 11 citations in OpenAlex.

  1. Article
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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 1 institution in 1 country.

Marc Christian HeßBiochemistry III, Department of Chemistry, Bielefeld University, Bielefeld, Germany.
Svenja BloessBiochemistry III, Department of Chemistry, Bielefeld University, Bielefeld, Germany.
Joe Max RisseFermentation Engineering, Faculty of Technology, Bielefeld University, Bielefeld, Germany.
Karl FriehsFermentation Engineering, Faculty of Technology, Bielefeld University, Bielefeld, Germany.
Gabriele Fischer von MollardBiochemistry III, Department of Chemistry, Bielefeld University, Bielefeld, Germany.ORCID 0000-0003-3236-1401
Bielefeld University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

l-amino acid oxidases (LAAOs) are flavoenzymes that catalyze the oxidative deamination of l-amino acids to the corresponding α-keto acids, ammonia, and hydrogen peroxide. Here, we show the overexpression, purification, and the characterization of LAAO4 from the fungus Hebeloma cylindrosporum in the yeast Pichia pastoris with a 9His-tag and compare this with the recently characterized 6His-hcLAAO4 expressed in E. coli. The expression of the enzyme with an ER-signal sequence in P. pastoris resulted in a glycosylated, secreted protein. The enzymatic activity without activation was higher after expression in P. pastoris compared to E. coli. Due to treatment with acidic pH, a striking increase of activity could be detected for both expression systems resulting in similar specific activities after acid activation. Regarding the substrate spectrum, temperature stability, K

Indexed as

Enzyme StabilityFermentationFungal ProteinsGene ExpressionHebelomaKineticsL-Amino Acid OxidasePichiaRecombinant ProteinsSubstrate SpecificityFungal ProteinsL-Amino Acid OxidaseRecombinant Proteins

Identifiers

PMID32852125
PMCPMC7568252
OpenAlexW3081161557

What OpenQuestion holds

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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.