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

Enhancement in catalytic activity of Aspergillus niger XynB by selective site-directed mutagenesis of active site amino acids.

Applied microbiology and biotechnology - 1 Jan 2018

Wu Xiuyun, Tian Zhennan, Jiang Xukai, Zhang Qun, Wang Lushan

Abstract excerpt

XynB from Aspergillus niger ATCC1015 (AnXynB) is a mesophilic glycoside hydrolase (GH) family 11 xylanase which holds great potentials in a wide variety of industrial applications. In the present study, the catalytic activity and stability of AnXynB were improved by a combination of computational and experimental approaches. Virtual mutation and molecular dynamics simulations indicated that the introduction of...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acids
Share to Aspergillus niger

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

Share to beta-Glucosidase

Share to Catalysis

Share to Catalytic Domain

Share to Endo-1,4-beta Xylanases

Share to Enzyme Stability

Share to Mutagenesis, Site-Directed

Source

Identifiers

PMID: 29103167
DOI: 10.1007/s00253-017-8607-8

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

Enhancement in catalytic activity of Aspergillus niger XynB by selective site-directed mutagenesis of active site amino acids.PMID 29103167Read ↗

Improving the Thermostability of Xylanase A from Bacillus subtilis by Combining Bioinformatics and Electrostatic Interactions Optimization.Semantic proximity Read ↗

Exploration of a N-terminal disulfide bridge to improve the thermostability of a GH11 xylanase from Aspergillus niger.Semantic proximity Read ↗

Mechanistic insights into activity-enhancing mutations from comparative analysis of two Bacillus subtilis GH11 xylanases.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 Properties of Xylanase from Alteromones Macleadii H35 Through Sequence Analysis.Semantic proximity Read ↗

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

Rational design of a thermophilic β-mannanase fromBacillus subtilis TJ-102 to improve its thermostability.Semantic proximity Read ↗

Thermostabilization of Bacillus subtilis GH11 xylanase by surface charge engineering.Semantic proximity Read ↗

Effect of the single mutation N9Y on the catalytical properties of xylanase Xyn11A from Cellulomonas uda: a biochemical and molecular dynamic simulation analysis.Semantic proximity Read ↗

Effects of helix and fingertip mutations on the thermostability of xyn11A investigated by molecular dynamics simulations and enzyme activity assays.Semantic proximity Read ↗

Structure-based mutagenesis of Penicillium griseofulvum xylanase using computational design.Semantic proximity Read ↗

Unleashing the Power of Evolution in Xylanase Engineering: Investigating the Role of Distal Mutation Regulation.Semantic proximity Read ↗

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