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 of the phytase from Escherichia coli and its extracellular production in bioreactors.

Applied microbiology and biotechnology - 1 Sept 2002

Miksch G, Kleist S, Friehs K, Flaschel E

Abstract excerpt

The gene for phytase from Escherichia coli was sequenced and compared with the appA gene. It was found to be a mutant derivative of the appA gene. After fusion with a C-terminal His-tag, phytase was purified by affinity chromatography and the enzymatic properties were analyzed. To develop a system for overexpression and extracellular production of phytase in E. coli, factors affecting the expression and secretion...

Read the complete abstract on PubMed

Topics

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

Share to Acid Phosphatase
Share to Bioreactors
Share to DNA, Bacterial

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Escherichia coli

Share to Escherichia coli Proteins

Share to Fermentation

Share to Kinetics

Share to Recombinant Proteins

Source

Identifiers

PMID: 12226725
DOI: 10.1007/s00253-002-1071-z

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

Overexpression of the phytase from Escherichia coli and its extracellular production in bioreactors.PMID 12226725Read ↗

Extracellular recombinant protein production from Escherichia coli.Semantic proximity Read ↗

Improving phytase enzyme activity in a recombinant phyA mutant phytase from Aspergillus niger N25 by error-prone PCR.Semantic proximity Read ↗

Engineering Protease-Resistant and Highly Active Phytases.Semantic proximity Read ↗

Engineered gene for Escherichia coli alkaline phosphatase for the construction of translational fusions.Semantic proximity Read ↗

Engineering Extracellular Expression Systems in Escherichia coli Based on Transcriptome Analysis and Cell Growth State.Semantic proximity Read ↗

Phytase producing lactic acid bacteria: Cell factories for enhancing micronutrient bioavailability of phytate rich foodsSemantic proximity Read ↗

β-Propeller phytases: Diversity, catalytic attributes, current developments and potential biotechnological applications.Semantic proximity Read ↗

Production of phytase under solid-state fermentation using Rhizopus oryzae: novel strain improvement approach and studies on purification and characterization.Semantic proximity Read ↗

Efficient production of extracellular proteins with Escherichia coli by means of optimized coexpression of bacteriocin release proteins.Semantic proximity Read ↗

Screening through the PLICable promoter toolbox enhances protein production in Escherichia coli.Semantic proximity Read ↗

Cloning of the Pseudomonas aeruginosa alkaline protease gene and secretion of the protease into the medium by Escherichia coli.Semantic proximity Read ↗

Increased efficiency of alkaline phosphatase production levels in Escherichia coli using a degenerate PelB signal sequence.Semantic proximity Read ↗

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