ArticleMicrobial cell factories2017
Directed evolution and secretory expression of a pyrethroid-hydrolyzing esterase with enhanced catalytic activity and thermostability.
Article in Microbial cell factories, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
15 citing papers in PubMed, 34 citations in OpenAlex.
- The ability of selected fungal strains to produce carboxylesterase enzymes for biodegradation and use of bifenthrin insecticide as carbon source: in vitro and in silico approaches.Bioprocess and biosystems engineering · 2024Article
- Degradation strategies of pesticide residue: From chemicals to synthetic biology.Synthetic and systems biotechnology · 2023Article
- Microbial elimination of pyrethroids: specific strains and involved enzymes.Applied microbiology and biotechnology · 2022Review
- Characterization and activity enhancement of a novel exo-type agarase Aga575 from Aquimarina agarilytica ZC1.Applied microbiology and biotechnology · 2021Article
- Biodegradation of fipronil: current state of mechanisms of biodegradation and future perspectives.Applied microbiology and biotechnology · 2021Review
- Novel Mechanism and Kinetics of Tetramethrin Degradation Using an IndigenousInternational journal of molecular sciences · 2021Article
- Pollutant Degrading Enzyme: Catalytic Mechanisms and Their Expanded Applications.Molecules (Basel, Switzerland) · 2021Review
- Current Approaches to and Future Perspectives on Methomyl Degradation in Contaminated Soil/Water Environments.Molecules (Basel, Switzerland) · 2020Review
- Random Mutagenesis by Insertion of Error-Prone PCR Products to the Chromosome ofFrontiers in microbiology · 2020Article
- Improvement of the catalytic activity and thermostability of a hyperthermostable endoglucanase by optimizing N-glycosylation sites.Biotechnology for biofuels · 2020Article
- Degradation of Acephate and Its Intermediate Methamidophos: Mechanisms and Biochemical Pathways.Frontiers in microbiology · 2020Review
- Combinatorial pathway enzyme engineering and host engineering overcomes pyruvate overflow and enhances overproduction of N-acetylglucosamine in Bacillus subtilis.Microbial cell factories · 2019Article
- Insight Into Microbial Applications for the Biodegradation of Pyrethroid Insecticides.Frontiers in microbiology · 2019Review
- Engineering the conserved and noncatalytic residues of a thermostable β-1,4-endoglucanase to improve specific activity and thermostability.Scientific reports · 2018Article
- Identification and immobilization of a novel cold-adapted esterase, and its potential for bioremediation of pyrethroid-contaminated vegetables.Microbial cell factories · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundPyrethroids are potentially harmful to human health and ecosystems. It is necessary to develop some efficient strategies to degrade pyrethroid residues. Biodegradation is generally considered as a safe, efficient, and inexpensive way to eliminate environmental contaminants. To date, although several pyrethroid-hydrolyzing esterases have been cloned, there has been no report about a pyrethroid hydrolase with high hydrolytic activity, good stability, and high productivity, indispensable enzymatic properties in practical biodegradation. Almost all pyrethroid hydrolases are intracellular enzymes, which require complex extraction protocols and present issues in terms of easy inactivation and low production.
resultsIn this study, random mutagenesis was performed on one pyrethroid-hydrolyzing esterase, Sys410, to enhance its activity and thermostability. Two beneficial mutations, A171V and D256N, were obtained by random mutagenesis and gave rise to the mutant M2. The mutant displayed ~1.5-fold improvement in the kcat/Km value and 2.46-fold higher catalytic activity. The optimal temperature was 10 °C higher than that of the wild-type enzyme (55 °C). The half-life at 40-65 °C was 3.3-310 times longer. It was surprising that M2 has a half-life of 12 h at 70 °C while Sys410 was completely inactivated at 70 °C. In addition, the desired gene was extracellularly expressed in a Pichia pastoris host system. The soluble expression level reached up to 689.7 mg/L. Remarkably, the enzyme could efficiently degrade various pyrethroids at moderate temperature for 15 min, exceeding a hydrolysis rate of 98%, which is the highest value ever reported.
conclusionsThis is the first report about random mutagenesis and secretory expression of pyrethroid-hydrolyzing esterase with high-level productivity and purity in P. pastoris. Broad substrate specificity, enhanced activity and thermostability make M2 an ideal candidate for the biodegradation of pyrethroid residues.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.