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

Characterizing pH-dependent stability profile of endo-β-mannanase enzyme: an in silico approach.

Journal of biomolecular structure & dynamics - 1 Nov 2025

Suryadihardja Gilbert, Suwanto Antonius, Yulandi Adi

Abstract excerpt

This research focuses on the characterization of four mannanase enzymes regarding their structure and stability across various pH conditions. The study employed in silico techniques, including homology modelling, protein superimposition, protonation state assignment, and molecular dynamics simulations, to analyze the enzyme's structure and behaviour. The results revealed distinct characteristics for each enzyme,...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Computer Simulation

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

Share to Enzyme Stability

Share to Hydrogen-Ion Concentration

Share to Models, Molecular

Share to Molecular Dynamics Simulation

Share to Mutation

Share to Protein Conformation

Source

Identifiers

PMID: 39616547
DOI: 10.1080/07391102.2024.2434032

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 17 Oct 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

Characterizing pH-dependent stability profile of endo-β-mannanase enzyme: an in silico approach.PMID 39616547Read ↗

A rational design for trypsin-resistant improvement of Armillariella tabescens β-mannanase MAN47 based on molecular structure evaluation.Semantic proximity Read ↗

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

Improving the kinetic stability of a hyperthermostable β-mannanase by a rationally combined strategy.Semantic proximity Read ↗

Improving the Catalytic Properties of Xylanase from Alteromones Macleadii H35 Through Sequence Analysis.Semantic proximity Read ↗

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

Modulating the pH-activity profile of cellulase A from Cellulomonas fimi by replacement of surface residues.Semantic proximity Read ↗

Probing impact of active site residue mutations on stability and activity of Neisseria polysaccharea amylosucrase.Semantic proximity Read ↗

Biology, Mechanism, and Structure of Enzymes in the α-d-Phosphohexomutase Superfamily.Semantic proximity Read ↗

Probing the stability of the modular family 10 xylanase from Rhodothermus marinus.Semantic proximity Read ↗

Engineering the pH-optimum of activity of the GH12 family endoglucanase by site-directed mutagenesis.Semantic proximity Read ↗

Mechanistic insights into activity-enhancing mutations from comparative analysis of two Bacillus subtilis GH11 xylanases.Semantic proximity Read ↗

Impact of the removal of N-terminal non-structured amino acids on activity and stability of xylanases from Orpinomyces sp. PC-2.Semantic proximity Read ↗

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