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

High yield production of a mutant Nippostrongylus brasiliensis acetylcholinesterase in Pichia pastoris and its purification.

Biotechnology and bioengineering - 5 Apr 2006

Richter Sven, Nieveler Jens, Schulze Holger, Bachmann Till T, Schmid Rolf D

Abstract excerpt

The mutant M301A of the acetylcholinesterase B from Nippostrongylus brasiliensis (NbAChE) was produced in a high-cell-density fermentation of a recombinant methylotrophic yeast Pichia pastoris. Dissolved oxygen (DO) spikes were used as an indicator for feeding the carbon source. Wet cell weight (WCW) reached after 8 days a maximum value of 316 g/L and the OD600 at this time was 280. The acetylcholinesterase...

Read the complete abstract on PubMed

Topics

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

Share to Acetylcholinesterase
Share to Biomass

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cholinesterase Inhibitors

Share to Chromatography, Gel

Share to Chromatography, Ion Exchange

Share to Fermentation

Share to Methanol

Share to Pichia

Source

Identifiers

PMID: 16302258
DOI: 10.1002/bit.20705

Genes

SDS

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

High yield production of a mutant Nippostrongylus brasiliensis acetylcholinesterase in Pichia pastoris and its purification.PMID 16302258Read ↗

Determinants of substrate specificity of a second non-neuronal secreted acetylcholinesterase from the parasitic nematode Nippostrongylus brasiliensis.Semantic proximity Read ↗

Insecticide detection through protein engineering of Nippostrongylus brasiliensis acetylcholinesterase B.Semantic proximity Read ↗

Expression and characterization of a codon-optimized butyrylcholinesterase for analysis of organophosphate insecticide residuesSemantic proximity Read ↗

Production of a sterol esterase from Ophiostoma piceae in batch and fed-batch bioprocesses using different Pichia pastoris phenotypes as cell factory.Semantic proximity Read ↗

Evaluation of Mut(S) and Mut⁺ Pichia pastoris strains for membrane-bound catechol-O-methyltransferase biosynthesis.Semantic proximity Read ↗

Recombinant protein expression in Pichia pastoris.Semantic proximity Read ↗

Acetylcholinesterase of Rhipicephalus (Boophilus) microplus and Phlebotomus papatasi: Gene identification, expression, and biochemical properties of recombinant proteinsSemantic proximity Read ↗

Optimization of the wheat puroindoline-a production in Pichia pastorisSemantic proximity Read ↗

High-level production and covalent immobilization of Providencia rettgeri penicillin G acylase (PAC) from recombinant Pichia pastoris for the development of a novel and stable biocatalyst of industrial applicability.Semantic proximity Read ↗

Expression of Soluble Ligand- and Antibody-binding Extracellular Domain of Human Muscle Acetylcholine Receptor α Subunit in Yeast Pichia pastorisSemantic proximity Read ↗

Functional expression of a blood tolerant laccase in Pichia pastoris.Semantic proximity Read ↗

Soluble, oligomeric, and ligand-binding extracellular domain of the human alpha7 acetylcholine receptor expressed in yeast: replacement of the hydrophobic cysteine loop by the hydrophilic loop of the ACh-binding protein enhances protein solubility.Semantic proximity Read ↗

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