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

The AXXXA motif: A rational design strategy and experimental studies to enhance both activity and thermostability of BTL2 lipase.

Enzyme and microbial technology - 1 Aug 2026

Ghorban Mahsa, Yakhchali Bagher, Rezaei Mehran Habibi, Aminzadeh Saeed, Haghbeen Kamahldin, Karkhanei Behrouz, Karkhane Ali Asghar

Abstract excerpt

Thermostability is a critical limitation for industrial lipases. Rational design using stabilizing structural motifs like AXXXA offers a targeted engineering approach. This study aimed to enhance both thermostability and catalytic efficiency of Bacillus thermocatenulatus lipase (BTL2) through computational design and experimental validation. Fifty potential AXXXA-forming mutations were screened in silico using...

Read the complete abstract on PubMed

Topics

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

Share to Bacterial Proteins
Share to Hydrogen-Ion Concentration

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

Share to Kinetics

Share to Models, Molecular

Share to Mutagenesis, Site-Directed

Share to Mutation

Share to Substrate Specificity

Share to Temperature

Source

Identifiers

PMID: 42085918
DOI: 10.1016/j.enzmictec.2026.110884

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

The AXXXA motif: A rational design strategy and experimental studies to enhance both activity and thermostability of BTL2 lipase.PMID 42085918Read ↗

Study of the effect of F17A mutation on characteristics of Bacillus thermocatenulatus lipase expressed in Pichia pastoris using in silico and experimental methods.Semantic proximity Read ↗

Predicting the impact of mutations on the specific activity of Bacillus thermocatenulatus lipase using a combined approach of docking and molecular dynamics.Semantic proximity Read ↗

[Improving the thermal stability of Bacillus subtilis lipase based on multiple computational design strategies].Semantic proximity Read ↗

Discovery of the Key Mutation Site Influencing the Thermostability of Thermomyces lanuginosus Lipase by Rosetta Design Programs.Semantic proximity Read ↗

A novel strategy to improve the thermostability of Penicillium camembertii mono- and di-acylglycerol lipase.Semantic proximity Read ↗

Exploring the protein stability landscape: Bacillus subtilis lipase A as a model for detergent tolerance.Semantic proximity Read ↗

Conversion of Bacillus thermocatenulatus lipase into an efficient phospholipase with increased activity towards long-chain fatty acyl substrates by directed evolution and rational design.Semantic proximity Read ↗

Automated optimization of the solubility of a hyper-stable α-amylase.Semantic proximity Read ↗

Enhancing thermostabilization of a newly discovered α-amylase from Bacillus cereus GL96 by combining computer-aided directed evolution and site-directed mutagenesis.Semantic proximity Read ↗

Significant improvement of the thermostability and catalytic efficiency of β-glucosidase Bgl59 via cysteine engineering and rational design.Semantic proximity Read ↗

In vitro evolved non-aggregating and thermostable lipase: structural and thermodynamic investigation.Semantic proximity Read ↗

Improving the catalytic activity and stability of Bacillus alcalophilus serine protease BAPB92 by rational design.Semantic proximity Read ↗

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