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

Characterization of a thermostable mutant of Agaricus brasiliensis laccase created by phylogeny-based design.

Journal of bioscience and bioengineering - 1 Dec 2017

Hamuro Yuhi, Tajima Katsuya, Matsumoto-Akanuma Akiko, Sakamoto Sayaka, Furukawa Ryutaro, Yamagishi Akihiko, Ohno Naohito, Akanuma Satoshi

Abstract excerpt

Laccases are enzymes that oxidize various aromatic compounds, and therefore they have attracted much attention from the standpoints of medical and industrial applications. We previously isolated the cDNA that codes for a laccase isozyme (Lac2a) from the medicinal mushroom Agaricus brasiliensis (Matsumoto-Akanuma et al., Int. J. Med. Mushrooms, 16, 375-393, 2014). In this study, we first attempted heterologous...

Read the complete abstract on PubMed

Topics

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

Share to Biocatalysis
Share to Enzyme Stability

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

Share to Hydrogen-Ion Concentration

Share to Laccase

Share to Mutant Proteins

Share to Oxidation-Reduction

Share to Pichia

Share to Protein Engineering

Source

Identifiers

PMID: 28847577
DOI: 10.1016/j.jbiosc.2017.07.004

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

Characterization of a thermostable mutant of Agaricus brasiliensis laccase created by phylogeny-based design.PMID 28847577Read ↗

A variant of Orpinomyces joyonii 1,3-1,4-beta-glucanase with increased thermal stability obtained by random mutagenesis and screening.Semantic proximity Read ↗

Protein Engineering Approaches to Enhance Fungal Laccase Production in S. cerevisiae.Semantic proximity Read ↗

Development of new laccases by directed evolution: functional and computational analyses.Semantic proximity Read ↗

Designing thermostable proteins: ancestral mutants of 3-isopropylmalate dehydrogenase designed by using a phylogenetic tree.Semantic proximity Read ↗

Engineering of a thermostable β-1,3-1,4-glucanase from Bacillus altitudinis YC-9 to improve its catalytic efficiency.Semantic proximity Read ↗

Widening the pH activity profile of a fungal laccase by directed evolution.Semantic proximity Read ↗

Bioinformatic analysis reveals high diversity of bacterial genes for laccase-like enzymes.Semantic proximity Read ↗

Rational design to improve thermostability and specific activity of the truncated Fibrobacter succinogenes 1,3-1,4-β-D-glucanase.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 ↗

Machine learning-guided multi-site combinatorial mutagenesis enhances the thermostability of pectin lyase.Semantic proximity Read ↗

Significant enhancement of the thermal stability and catalytic efficiency of transglutaminase in Streptomyces mobaraensis engineered through the novel S. mobaraensis genomic mutant library construction method GHR/Sml.Semantic proximity Read ↗

Tuning Thermostability and Catalytic Efficiency of Aflatoxin-Degrading Enzyme by Error-prone PCR.Semantic proximity Read ↗

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