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

Enhancing the thermostability of a cold-active lipase from Penicillium cyclopium by in silico design of a disulfide bridge.

Applied biochemistry and biotechnology - 1 Aug 2014

Tan Zhongbiao, Li Jianfang, Wu Minchen, Wang Junqing

Abstract excerpt

Cysteine mutants of a cold-active lipase (PcLipI) from Penicillium cyclopium were designed by the software Disulfide by Design Ver. 1.20 in an effort to improve enzyme thermostability by addition of a disulfide bridge. Those mutants predicted by molecular dynamics simulation to have better thermostability than the wild type were first expressed in Escherichia coli BL21(DE3) and then, for further investigation, in...

Read the complete abstract on PubMed

Topics

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

Share to Computer Simulation
Share to Enzyme Stability

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

Share to Escherichia coli

Share to Models, Molecular

Share to Mutation

Share to Protein Conformation

Share to Recombinant Proteins

Share to Software

Source

Identifiers

PMID: 24867629
DOI: 10.1007/s12010-014-0962-7

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

Enhancing the thermostability of a cold-active lipase from Penicillium cyclopium by in silico design of a disulfide bridge.PMID 24867629Read ↗

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

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

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

Improving thermostability of (R)-selective amine transaminase from Aspergillus terreus through introduction of disulfide bonds.Semantic proximity Read ↗

Engineering of a thermo-alkali-stable lipase from Rhizopus chinensis by rational design of a buried disulfide bond and combinatorial mutagenesis.Semantic proximity Read ↗

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

Enhancing the thermostability of transglutaminase from Streptomyces mobaraensis based on the rational design of a disulfide bond.Semantic proximity Read ↗

Computational approach for designing thermostable Candida antarctica lipase B by molecular dynamics simulation.Semantic proximity Read ↗

The effect of disulfide bond introduction and related Cys/Ser mutations on the stability of a cyclohexanone monooxygenase.Semantic proximity Read ↗

Engineering and introduction of de novo disulphide bridges in organophosphorus hydrolase enzyme for thermostability improvement.Semantic proximity Read ↗

A thermostable phospholipase C obtained by consensus designSemantic proximity Read ↗

Enhancement of protein thermostability by three consecutive mutations using loop-walking method and machine learning.Semantic proximity Read ↗

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