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

[A rational loop region engineering strategy for enhancing the thermostability of chondroitinase ABC].

Sheng wu gong cheng xue bao = Chinese journal of biotechnology - 25 Mar 2026

Yang Ying, Li Chunqing, Zhang Jing, Zeng Yan, Teng Yu'ou, Li Ming, Zhu Yueming, Sun Yuanxia

Abstract excerpt

Chondroitinase ABC (ChABC) holds significant value in biomedical applications and polysaccharide structure analysis. However, the poor thermostability of this enzyme severely limits its industrial production and utilization. Focusing on the multidomain characteristics of PvChABC derived from Proteus vulgaris and targeting the loop region connecting the N-terminal domain and the catalytic domain, we obtained an...

Read the complete abstract on PubMed

Topics

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

Share to Enzyme Stability
Share to Molecular Dynamics Simulation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutation

Share to Protein Engineering

Source

Identifiers

PMID: 41873075
DOI: 10.13345/j.cjb.250622

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

[A rational loop region engineering strategy for enhancing the thermostability of chondroitinase ABC].PMID 41873075Read ↗

Semi-rational design of the N-terminal of Chondroitinase ABC to improve the catalytic activity.Semantic proximity Read ↗

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

Role of His-His interaction in Ser474-His475-Tyr476 sequence of chondroitinase ABC I in the enzyme activity and stability.Semantic proximity Read ↗

Hook loop dynamics engineering transcended the barrier of activity-stability trade-off and boosted the thermostability of enzymes.Semantic proximity Read ↗

Enhancing the specific activity of 3α-hydroxysteroid dehydrogenase through cross-regional combinatorial mutagenesis.Semantic proximity Read ↗

Thermostability Enhancement of Streptomyces mobaraensis Transglutaminase by Folding Free Energy-Guided Helix-Corner Motif Engineering.Semantic proximity Read ↗

Insights into the structural characteristics and substrate binding analysis of chondroitin AC lyase (PsPL8A) from Pedobacter saltans.Semantic proximity Read ↗

Semi-rational design in simultaneous improvement of thermostability and activity of β-1,3-glucanase from Alkalihalobacillus clausii KSMK16.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 ↗

Computer-assisted semi-rational design enhanced the enzymatic activity and protein stability of Proteinase K in calcium-free conditions.Semantic proximity Read ↗

Improving the thermal stability and catalytic activity of ulvan lyase by the combination of FoldX and KnowVolution campaign.Semantic proximity Read ↗

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

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