Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Purification and characteristics of xyloglucanase and five other cellulolytic enzymes from Trichoderma reesei QM9414.

Biochemistry. Biokhimiia - 1 Apr 2013

Qi Huan, Bai Fali, Liu Aihua

Abstract excerpt

By combining anion-exchange chromatography with gel filtration, an effective method for purification of wild-type xyloglucanase and five other cellulolytic enzymes from strain QM9414 of Trichoderma reesei was established. Characterization by enzyme activity assay, SDS-PAGE, and mass spectrometry identified the purified proteins as cellobiohydrolases I and II, endoglucanases I and II, a xyloglucanase, and...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Chromatography, Gel
Share to Chromatography, Ion Exchange
Share to Enzyme Activation

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Glycoside Hydrolases

Share to Mutation

Share to Substrate Specificity

Share to Trichoderma

Share to Xylosidases

Source

Identifiers

PMID: 23590446
DOI: 10.1134/S0006297913040123

Genes

SDS

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Purification and characteristics of xyloglucanase and five other cellulolytic enzymes from Trichoderma reesei QM9414.PMID 23590446Read ↗

Deciphering the molecular mechanisms behind cellulase production in Trichoderma reesei, the hyper-cellulolytic filamentous fungus.Semantic proximity Read ↗

Trichoderma reesei xylanase 5 is defective in the reference strain QM6a but functional alleles are present in other wild-type strains.Semantic proximity Read ↗

A β-glucosidase hyper-production Trichoderma reesei mutant reveals a potential role of cel3D in cellulase production.Semantic proximity Read ↗

Efficient Isolation and Characterization of a Cellulase Hyperproducing Mutant Strain of Trichoderma reesei.Semantic proximity Read ↗

Identification and purification of the main components of cellulases from a mutant strain of Trichoderma viride T 100-14.Semantic proximity Read ↗

Quantitative secretomic analysis of Trichoderma reesei strains reveals enzymatic composition for lignocellulosic biomass degradation.Semantic proximity Read ↗

A novel Trichoderma reesei mutant RP698 with enhanced cellulase production.Semantic proximity Read ↗

Cellulase hyperproducing mutants derived from the fungus Trichoderma reesei QM9414 produced large amounts of cellulase at the enzymatic and transcriptional levels.Semantic proximity Read ↗

Xylanase gene transcription in Trichoderma reesei is triggered by different inducers representing different hemicellulosic pentose polymers.Semantic proximity Read ↗

RNAi-Mediated Gene Silencing of Trcot1 Induces a Hyperbranching Phenotype in Trichoderma reesei.Semantic proximity Read ↗

Genomics insights into different cellobiose hydrolysis activities in two Trichoderma hamatum strains.Semantic proximity Read ↗

Array comparative genomic hybridization analysis of Trichoderma reesei strains with enhanced cellulase production properties.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.