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

Evaluation of chitosan-binding amino acid residues of chitosanase from Paenibacillus fukuinensis.

Bioscience, biotechnology, and biochemistry - 1 Jan 2014

Isogawa Danya, Morisaka Hironobu, Kuroda Kouichi, Kusaoke Hideo, Kimoto Hisashi, Suye Shin-Ichiro, Ueda Mitsuyoshi

Abstract excerpt

Chitosan oligosaccharides longer than a hexamer have higher bioactivity than polymer or shorter oligosaccharides, such as the monomer or dimer. In our previous work, we generated Paenibacillus fukuinensis chitosanase-displaying yeast using yeast cell surface displaying system and demonstrated the catalytic base. Here we investigated the specific function of putative four amino acid residues Trp159, Trp228,...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Substitution
Share to Chitosan

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Glycoside Hydrolases

Share to Hydrolysis

Share to Models, Molecular

Share to Mutation

Share to Protein Binding

Share to Protein Conformation

Source

Identifiers

PMID: 25229853
DOI: 10.1080/09168451.2014.917263

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Evaluation of chitosan-binding amino acid residues of chitosanase from Paenibacillus fukuinensis.PMID 25229853Read ↗

Protein-engineering of chitosanase from Bacillus sp. MN to alter its substrate specificity.Semantic proximity Read ↗

Structural insights into the substrate-binding mechanism for a novel chitosanase.Semantic proximity Read ↗

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

Biochemical insights into the key residue substituents of an L-asparaginase from Thermococcus kodakarensis and their application in acrylamide mitigation.Semantic proximity Read ↗

A highly Conserved Aspartic Acid Residue of the Chitosanase from Bacillus Sp. TS Is Involved in the Substrate Binding.Semantic proximity Read ↗

Chitosanases from Family 46 of Glycoside Hydrolases: From Proteins to Phenotypes.Semantic proximity Read ↗

Enhancing the catalytic activity of a GH5 processive endoglucanase from Bacillus subtilis BS-5 by site-directed mutagenesis.Semantic proximity Read ↗

Selection and mutational analyses of the substrate interacting residues of a chitinase from Enterobacter cloacae subsp. cloacae (EcChi2) to improve transglycosylation.Semantic proximity Read ↗

Improve thermostability of Bacillus sp. TS chitosanase through structure-based alignment.Semantic proximity Read ↗

Aromatic residues in the catalytic center of chitinase A from Serratia marcescens affect processivity, enzyme activity, and biomass converting efficiency.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 ↗

Structural features of Aspergillus niger β-galactosidase define its activity against glycoside linkages.Semantic proximity Read ↗

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