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

Overexpression, purification, and characterization of Paenibacillus cell surface-expressed chitinase ChiW with two catalytic domains.

Bioscience, biotechnology, and biochemistry - 1 Jan 2014

Itoh Takafumi, Sugimoto Ikumi, Hibi Takao, Suzuki Fumiko, Matsuo Koichi, Fujii Yutaka, Taketo Akira, Kimoto Hisashi

Abstract excerpt

Paenibacillus sp. strain FPU-7 produces several different chitinases and effectively hydrolyzes robust chitin. Among the P. FPU-7 chitinases, ChiW, a novel monomeric chitinase with a molecular mass of 150 kDa, is expressed as a cell surface molecule. Here, we report that active ChiW lacking the anchoring domains in the N-terminus was successfully overproduced in Escherichia coli and purified to homogeneity. The...

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 Catalytic Domain

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

Share to Chitin

Share to Chitinases

Share to Escherichia coli

Share to Gene Expression

Share to Mutagenesis

Share to Substrate Specificity

Source

Identifiers

PMID: 25036959
DOI: 10.1080/09168451.2014.891935

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

Overexpression, purification, and characterization of Paenibacillus cell surface-expressed chitinase ChiW with two catalytic domains.PMID 25036959Read ↗

Fungal chitinases: diversity, mechanistic properties and biotechnological potential.Semantic proximity Read ↗

Molecular characterization of an endochitinase from Bacillus thuringiensis subsp. konkukianSemantic proximity Read ↗

The C-terminal module of Chi1 from Aeromonas caviae CB101 has a function in substrate binding and hydrolysis.Semantic proximity Read ↗

Active-site mutations improved the transglycosylation activity of Stenotrophomonas maltophilia chitinase A.Semantic proximity Read ↗

Crystal structure and enzymatic properties of a bacterial family 19 chitinase reveal differences from plant enzymes.Semantic proximity Read ↗

Cloning and high-level production of a chitinase from Chromobacterium sp. and the role of conserved or nonconserved residues on its catalytic activity.Semantic proximity Read ↗

Inverse relationship between chitobiase and transglycosylation activities of chitinase-D from Serratia proteamaculans revealed by mutational and biophysical analyses.Semantic proximity Read ↗

Mutation of active site residues in the chitin-binding domain ChBDChiA1 from chitinase A1 of Bacillus circulans alters substrate specificity: use of a green fluorescent protein binding assay.Semantic proximity Read ↗

Engineering Bacterial Chitinases for Industrial Application: From Protein Engineering to Bacterial Strains Mutation! A Comprehensive Review of Physical, Molecular, and Computational Approaches.Semantic proximity Read ↗

Purification and characterization of a chitinase from Serratia proteamaculansSemantic proximity Read ↗

Improvement of chitinase Pachi with nematicidal activities by random mutagenesis.Semantic proximity Read ↗

Sequence analysis and docking performance of extracellular chitinase from Bacillus pumilus MCB-7, a novel mangrove isolate.Semantic proximity Read ↗

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