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

Topics Community

Article

One-step immobilization of mutant TvDAAO yields an active and stable biocatalyst in extreme conditions.

Bioprocess and biosystems engineering - 1 Aug 2026

Atroshenko Denis L, Vlasova Maria A, Shelomov Mikhail D, Pometun Anastasia A, Savin Svyatoslav S, Tishkov Vladimir I

Abstract excerpt

D-Amino acid oxidase (DAAO) is an important enzyme in modern biotechnology, used for synthetic, analytical, and medical purposes. Numerous mutant forms of DAAO with different properties have been described previously. Recently, we combined six beneficial amino acid substitutions in DAAO from Trigonopsis variabilis (TvDAAO) to create the multipoint mutant TvDAAO E32R/F33D/F54S/C108F/M156L/C298N (mut-TvDAAO)....

Topics

Join the communities discussing this publication.

Cephalosporins
Enzyme Stability
Fungal Proteins
Hydrogen-Ion Concentration
Hydrogen Peroxide

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 42440129
DOI: 10.1007/s00449-026-03386-8

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 31 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

0

discussions

0

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

One-step immobilization of mutant TvDAAO yields an active and stable biocatalyst in extreme conditions.PMID 42440129Read ↗

Engineering of substrate specificity of D-amino acid oxidase from the yeast Trigonopsis variabilis: directed mutagenesis of Phe258 residue.Semantic proximity Read ↗

Distal mutations enhance efficiency of free and immobilized NOV1 dioxygenase for vanillin synthesis.Semantic proximity Read ↗

Evolution of Glucose Dehydrogenase for Cofactor Regeneration in Bioredox Processes with Denaturing Agents.Semantic proximity Read ↗

Mechanistic and Crystallographic Studies of Azoreductase AzoA from Bacillus wakoensis A01.Semantic proximity Read ↗

Gradually accumulating beneficial mutations to improve the thermostability of N-carbamoyl-D-amino acid amidohydrolase by step-wise evolution.Semantic proximity Read ↗

Engineering the substrate specificity of D-amino-acid oxidase.Semantic proximity Read ↗

Enhanced Thermostability and Catalytic Efficiency of Alginate Lyase Alyw203 by Hydrogen Bond Network Reconstruction.Semantic proximity Read ↗

Efficient biomanufacturing of vitamin E succinate in non-aqueous media via synergistic computational evolution and immobilization of lipase.Semantic proximity Read ↗

Modulating D-amino acid oxidase substrate specificity: production of an enzyme for analytical determination of all D-amino acids by directed evolution.Semantic proximity Read ↗

Modification of galactitol dehydrogenase from Rhodobacter sphaeroides D for immobilization on polycrystalline gold surfaces.Semantic proximity Read ↗

Extreme makeover: Engineering the activity of a thermostable alcohol dehydrogenase (AdhD) from Pyrococcus furiosus.Semantic proximity Read ↗

A Diamine Oxidase from <em>Glutamicibacter halophytocola</em> for the Degradation of Histamine and Tyramine in FoodsSemantic proximity Read ↗

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