Evidence map›Paper›PMID 26285758›Full record

ArticleMolecular biotechnology2015

Recombinant Expression of Trichoderma reesei Cel61A in Pichia pastoris: Optimizing Yield and N-terminal Processing.

Magali Tanghe, Barbara Danneels, Andrea Camattari, Anton Glieder, Isabel Vandenberghe, Bart Devreese, Ingeborg Stals, Tom Desmet

Abstract read
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In one paragraph

Article in Molecular biotechnology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

25 citing papers in PubMed, 82 citations in OpenAlex.

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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

8 authors at 3 institutions in 3 countries.

Magali TangheLaboratory of Industrial Biotechnology and Biocatalysis, Department of Biochemical and Microbial Technology, Ghent University, Coupure Links 653, 9000, Ghent, Belgium. Magali.Tanghe@ugent.be.
Barbara DanneelsLaboratory of Industrial Biotechnology and Biocatalysis, Department of Biochemical and Microbial Technology, Ghent University, Coupure Links 653, 9000, Ghent, Belgium.
Andrea CamattariBioprocessing Technology Institute, A*STAR (Agency for Science, Technology and Research), 20 Biopolis Way, #06-01, Centros, 138668, Singapore.
Anton GliederInstitute of Molecular Biotechnology, NAWI Graz, Graz University of Technology, Petersgasse 14, 8010, Graz, Austria.
Isabel VandenbergheLaboratory of Protein Biochemistry and Biomolecular Engineering, Department of Biochemistry and Microbiology, Ghent University, K.L. Ledeganckstraat 35, 9000, Ghent, Belgium.
Bart DevreeseLaboratory of Protein Biochemistry and Biomolecular Engineering, Department of Biochemistry and Microbiology, Ghent University, K.L. Ledeganckstraat 35, 9000, Ghent, Belgium.
Ingeborg StalsBioTec Laboratory, Department of Applied Biosciences, Ghent University, V. Vaerwijckweg 1, 9000, Ghent, Belgium.
Tom DesmetLaboratory of Industrial Biotechnology and Biocatalysis, Department of Biochemical and Microbial Technology, Ghent University, Coupure Links 653, 9000, Ghent, Belgium.
Ghent University · BEBioprocessing Technology Institute · SGGraz University of Technology · AT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The auxiliary activity family 9 (AA9, formerly GH61) harbors a recently discovered group of oxidative enzymes that boost cellulose degradation. Indeed, these lytic polysaccharide monooxygenases (LPMOs) are able to disrupt the crystalline structure of cellulose, thereby facilitating the work of hydrolytic enzymes involved in biomass degradation. Since these enzymes require an N-terminal histidine residue for activity, their recombinant production as secreted protein is not straightforward. We here report the expression optimization of Trichoderma reesei Cel61A (TrCel61A) in the host Pichia pastoris. The use of the native TrCel61A secretion signal instead of the alpha-mating factor from Saccharomyces cerevisiae was found to be crucial, not only to obtain high protein yields (>400 mg/L during fermentation) but also to enable the correct processing of the N-terminus. Furthermore, the LPMO activity of the enzyme is demonstrated here for the first time, based on its degradation profile of a cellulosic substrate.

Indexed as

Amino Acid SequenceBiomassCelluloseDNA, FungalFermentationFungal ProteinsHydrolysisMating FactorMixed Function OxygenasesMolecular Sequence DataPeptidesPichiaPolysaccharidesSaccharomyces cerevisiaeSequence Analysis, DNATrichodermaCelluloseDNA, FungalFungal ProteinsMating FactorMixed Function OxygenasesPeptidesPolysaccharidesAuxiliary activity family 9Cellulose hydrolysisLytic polysaccharide monooxygenaseN-terminal processingPichia pastorisTrichoderma reesei Cel61A (TrCel61A)

Identifiers

PMID26285758
OpenAlexW2150544704

What OpenQuestion holds

Textmetadata
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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.