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

Functional expression and stabilization of horseradish peroxidase by directed evolution in Saccharomyces cerevisiae.

Biotechnology and bioengineering - 1 Sept 2001

Morawski B, Quan S, Arnold F H

Abstract excerpt

Biotechnology applications of horseradish peroxidase (HRP) would benefit from access to tailor-made variants with greater specific activity, lower K(m) for peroxide, and higher thermostability. Starting with a mutant that is functionally expressed in Saccharomyces cerevisiae, we used random mutagenesis, recombination, and screening to identify HRP-C mutants that are more active and stable to incubation in...

Read the complete abstract on PubMed

Topics

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

Share to Directed Molecular Evolution
Share to Enzyme Stability
Share to Half-Life

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

Share to Horseradish Peroxidase

Share to Hot Temperature

Share to Hydrogen Peroxide

Share to Isoenzymes

Share to Isoleucine

Source

Identifiers

PMID: 11505379
DOI: 10.1002/bit.1149

Genes

SDS

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

Functional expression and stabilization of horseradish peroxidase by directed evolution in Saccharomyces cerevisiae.PMID 11505379Read ↗

Consensus mutagenesis reveals that non-helical regions influence thermal stability of horseradish peroxidase.Semantic proximity Read ↗

Effects of single mutations on the stability of horseradish peroxidase to hydrogen peroxide.Semantic proximity Read ↗

Investigating the structural and functional effects of mutating Asn glycosylation sites of horseradish peroxidase to Asp.Semantic proximity Read ↗

Glyco-variant library of the versatile enzyme horseradish peroxidase.Semantic proximity Read ↗

Selection of horseradish peroxidase variants with enhanced enantioselectivity by yeast surface display.Semantic proximity Read ↗

Effects of mutations in the helix G region of horseradish peroxidase.Semantic proximity Read ↗

Evolving thermostability in mutant libraries of ligninolytic oxidoreductases expressed in yeast.Semantic proximity Read ↗

Improving the thermal stability of lactate oxidase by directed evolution.Semantic proximity Read ↗

Structural and kinetic studies of a series of mutants of galactose oxidase identified by directed evolution.Semantic proximity Read ↗

Combining Protein and Strain Engineering for the Production of Glyco-Engineered Horseradish Peroxidase C1A in Pichia pastoris.Semantic proximity Read ↗

Directed evolution of glucose oxidase from Aspergillus niger for ferrocenemethanol-mediated electron transfer.Semantic proximity Read ↗

Enzymatic improvement of mitochondrial thiol oxidase Erv1 for oxidized glutathione fermentation by Saccharomyces cerevisiae.Semantic proximity Read ↗

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