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

Improvements in Glucose Sensitivity and Stability of Trichoderma reesei β-Glucosidase Using Site-Directed Mutagenesis.

PloS one - 1 Jan 2016

Guo Boyang, Amano Yoshihiko, Nozaki Kouichi

Abstract excerpt

Glucose sensitivity and pH and thermal stabilities of Trichoderma reesei Cel1A (Bgl II) were improved by site-directed mutagenesis of only two amino acid residues (L167W or P172L) at the entrance of the active site. The Cel1A mutant showed high glucose tolerance (50% of inhibitory concentration = 650 mM), glucose stimulation (2.0 fold at 50 mM glucose), and enhanced specific activity (2.4-fold) compared with...

Read the complete abstract on PubMed

Topics

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

Share to beta-Glucosidase
Share to Catalytic Domain
Share to Enzyme Stability

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

Share to Glucose

Share to Glucose Tolerance Test

Share to Glucosides

Share to Sweetening Agents

Share to Trichoderma

Source

Open in PubMed Open full text

Identifiers

PMID: 26790148
DOI: 10.1371/journal.pone.0147301
PMCID: PMC4720395

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

Improvements in Glucose Sensitivity and Stability of Trichoderma reesei β-Glucosidase Using Site-Directed Mutagenesis.PMID 26790148Read ↗

Mutations in the substrate entrance region of β-glucosidase from Trichoderma reesei improve enzyme activity and thermostability.Semantic proximity Read ↗

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

Engineering endoglucanase II from Trichoderma reesei to improve the catalytic efficiency at a higher pH optimum.Semantic proximity Read ↗

Single Mutation in Transcriptional Activator Xyr1 Enhances Cellulase and Xylanase Production in Trichoderma reesei on Glucose.Semantic proximity Read ↗

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

From in silico to in vitro: modelling and production of Trichoderma reesei endoglucanase 1 and its mutant in Pichia pastoris.Semantic proximity Read ↗

Improvement of Trichoderma reesei xylanase II thermal stability by serine to threonine surface mutations.Semantic proximity Read ↗

Engineering the conserved and noncatalytic residues of a thermostable β-1,4-endoglucanase to improve specific activity and thermostability.Semantic proximity Read ↗

Cellulase production on glucose-based media by the UV-irradiated mutants of Trichoderma reesei.Semantic proximity Read ↗

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

Engineering highly thermostable xylanase variants using an enhanced combinatorial library method.Semantic proximity Read ↗

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

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