ArticleBioresources and bioprocessing2019
Accelerated directed evolution of dye-decolorizing peroxidase using a bacterial extracellular protein secretion system (BENNY).
Article in Bioresources and bioprocessing, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
9 citing papers in PubMed, 30 citations in OpenAlex.
- Review
- Computational Studies of Enzymes for C-F Bond Degradation and Functionalization.Chemphyschem : a European journal of chemical physics and physical chemistry · 2025Review
- Hyperthermophilic xylanase and thermophilicity analysis by molecular dynamic simulation with quantum mechanics.Applied microbiology and biotechnology · 2024Article
- Electrochemical Actuation of a DyP Peroxidase: A Facile Method for Drastic Improvement of the Catalytic Performance.ACS catalysis · 2023Article
- Engineering Ag43 Signal Peptides with Bacterial Display and Selection.Methods and protocols · 2022Article
- Efficient degradation of various emerging pollutants by wild type and evolved fungal DyP4 peroxidases.PloS one · 2022Article
- Challenges and Recent Advances in Enzyme-Mediated Wastewater Remediation-A Review.Nanomaterials (Basel, Switzerland) · 2021Review
- Mutational and structural analysis of an ancestral fungal dye-decolorizing peroxidase.The FEBS journal · 2021Article
- Random and combinatorial mutagenesis for improved total production of secretory target protein in Escherichia coli.Scientific reports · 2021Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundDye-decolorizing peroxidases (DyPs) are haem-containing peroxidases that show great promises in industrial biocatalysis and lignocellulosic degradation. Through the use of
resultAfter 3 rounds of random mutagenesis with error-prone polymerase chain reaction (epPCR) and 1 round of saturation mutagenesis, we obtained 4D4 variant (I56V, K109R, N227S and N312S) that displays multiple desirable phenotypes, including higher protein yield and secretion, higher specific activity (2.7-fold improvement in
conclusionTo our best knowledge, this is the first report of applying OsmY to simplify the directed evolution workflow and to direct the extracellular secretion of a haem protein such as DyP4.
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Registered trials
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