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

Sustainable bio-finishing of denim fabric using a novel thermostable cellulase from mutant Bacillus subtilis IE3 for reduced environmental impact.

International journal of biological macromolecules - 1 Apr 2026

Demirkan Elif, Kut Dilek, Karakaya Ersin, Yıldırım Irem, Liaqat Fakhra, Khazi Mahammed Ilyas

Abstract excerpt

Innovation in environmentally friendly textile processing is largely dependent on thermostable and effective cellulases. This study describes the production and functional evaluation of a thermotolerant cellulase derived from the mutant Bacillus subtilis IE3, generated via ethyl methanesulfonate (EMS) mutagenesis of the novel B. subtilis 171ES strain. The mutant exhibited an 82% increase in cellulase production...

Read the complete abstract on PubMed

Topics

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

Share to Bacillus subtilis
Share to Cellulase

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Enzyme Stability

Share to Hydrogen-Ion Concentration

Share to Kinetics

Share to Mutation

Share to Temperature

Source

Identifiers

PMID: 41786197
DOI: 10.1016/j.ijbiomac.2026.151223

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Sustainable bio-finishing of denim fabric using a novel thermostable cellulase from mutant Bacillus subtilis IE3 for reduced environmental impact.PMID 41786197Read ↗

Enhancing the catalytic activity of a GH5 processive endoglucanase from Bacillus subtilis BS-5 by site-directed mutagenesis.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 ↗

Two-step computational redesign of Bacillus subtilis cellulase and β-glucanase for enhanced thermostability and activity.Semantic proximity Read ↗

A surface immobilization method of endoglucanase from Cellulomonas biazotea mutant improved catalytic properties of biocatalyst during processing.Semantic proximity Read ↗

Insights into the Catalytic Mechanism of a Novel XynA and Structure-Based Engineering for Improving Bifunctional Activities.Semantic proximity Read ↗

Improving the catalytic activity of β-glucosidase from Coniophora puteana via semi-rational design for efficient biomass cellulose degradation.Semantic proximity Read ↗

Rational design to improve thermostability and specific activity of the truncated Fibrobacter succinogenes 1,3-1,4-β-D-glucanase.Semantic proximity Read ↗

Clostridium thermocellum thermostable lichenase with circular permutations and modifications in the N-terminal region retains its activity and thermostability.Semantic proximity Read ↗

Cellulase production in a new mutant strain of Penicillium decumbens ML-017 by solid state fermentation with rice bran.Semantic proximity Read ↗

Structure-Guided Engineering Unveils Deeper Substrate Channel in Processive Endoglucanase EG5C-1 Contributing to Enhanced Catalytic Efficiency and Processivity.Semantic proximity Read ↗

A versatile esterase from Bacillus subtilis: cloning, expression, characterization, and its application in biocatalysis.Semantic proximity Read ↗

Insights into enhanced thermostability of a cellulosomal enzyme.Semantic proximity Read ↗

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