Evidence map›Paper›PMID 22355001›Full record

ArticleMolecular & cellular proteomics : MCP2012

Quantitative secretomic analysis of Trichoderma reesei strains reveals enzymatic composition for lignocellulosic biomass degradation.

Sunil S Adav, Lim Tze Chao, Siu Kwan Sze

Abstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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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

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3 · Its place in the literature

Who cites it

50 citing papers in PubMed.

  1. Article
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  13. The Change in the Composition ofMicrobiology insights · 2019
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4 · The record

Corrections and comments

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5 · Who and what money

Authors and funding

3 authors.

Sunil S AdavSchool of Biological Sciences, Nanyang Technological University, Singapore.
Lim Tze Chao
Siu Kwan Sze

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Trichoderma reesei is a mesophilic, filamentous fungus, and it is a major industrial source of cellulases, but its lignocellulolytic protein expressions on lignocellulosic biomass are poorly explored at present. The extracellular proteins secreted by T. reesei QM6a wild-type and hypercellulolytic mutant Rut C30 grown on natural lignocellulosic biomasses were explored using a quantitative proteomic approach with 8-plex high throughput isobaric tags for relative and absolute quantification (iTRAQ) and analyzed by liquid chromatography tandem mass spectrometry. We quantified 230 extracellular proteins, including cellulases, hemicellulases, lignin-degrading enzymes, proteases, protein-translocating transporter, and hypothetical proteins. Quantitative iTRAQ results suggested that the expressions and regulations of these lignocellulolytic proteins in the secretome of T. reesei wild-type and mutant Rut C30 were dependent on both nature and complexity of different lignocellulosic carbon sources. Therefore, we discuss here the essential lignocellulolytic proteins for designing an enzyme mixture for optimal lignocellulosic biomass hydrolysis.

Indexed as

BiomassCarrier ProteinsCellulasesChromatography, LiquidFungal ProteinsGene Expression Regulation, FungalHydrolysisLigninMultigene FamilyMutationPeptide HydrolasesProteomicsTandem Mass SpectrometryTrichodermaCarrier ProteinsCellulasesFungal ProteinsLigninlignocellulosePeptide Hydrolases

Identifiers

PMID22355001
PMCPMC3394936

What OpenQuestion holds

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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.