ArticleApplied and environmental microbiology2014
Newly identified thermostable esterase from Sulfobacillus acidophilus: properties and performance in phthalate ester degradation.
Article in Applied and environmental microbiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 98 citations in OpenAlex.
- Biological Degradation of Phthalates: From Bioremediation to Plastic Waste Valorization.ChemSusChem · 2026Review
- Identification and Characterization of a Novel Di-(2-ethylhexyl) Phthalate Hydrolase from a Marine Bacterial StrainInternational journal of molecular sciences · 2025Article
- Biodegradation of short-chain phthalate esters (PAEs) by Sinomonas sp. S2 isolated from a soil contaminated by metal(loid)s smelting.Biodegradation · 2025Article
- Identification and characterisation of moderately thermostable diisobutyl phthalate degrading esterase from a Great Artesian BasinBiotechnology reports (Amsterdam, Netherlands) · 2024Article
- Review
- Whole-genome analysis of3 Biotech · 2023Article
- A Novel and Efficient Phthalate Hydrolase fromMolecules (Basel, Switzerland) · 2023Article
- Phthalate Esters Metabolic StrainMicroorganisms · 2022Article
- Enzyme catalyzes ester bond synthesis and hydrolysis: The key step for sustainable usage of plastics.Frontiers in microbiology · 2022Review
- Enhanced esterase activity during the degradation of dibutyl phthalate by Fusarium species in liquid fermentation.Journal of industrial microbiology & biotechnology · 2021Article
- Article
- Identification and Heterologous Production of a Lipase from Geobacillus kaustophilus DSM 7263The protein journal · 2021Article
- Induction of esterase activity during the degradation of high concentrations of the contaminant di(2-ethylhexyl) phthalate by3 Biotech · 2020Article
- Development of a whole-cell biocatalyst for diisobutyl phthalate degradation by functional display of a carboxylesterase on the surface of Escherichia coli.Microbial cell factories · 2020Article
- Characterization of a novel family VIII esterase EstM2 from soil metagenome capable of hydrolyzing estrogenic phthalates.Microbial cell factories · 2020Article
- Article
- N-terminal domain replacement changes an archaeal monoacylglycerol lipase into a triacylglycerol lipase.Biotechnology for biofuels · 2019Article
- Excellent Degradation Performance of a Versatile Phthalic Acid Esters-Degrading Bacterium and Catalytic Mechanism of Monoalkyl Phthalate Hydrolase.International journal of molecular sciences · 2018Article
- Characterization and Genome Analysis of a Phthalate Esters-Degrading StrainBioMed research international · 2018Article
- Characterization and Genomic Analysis of a Highly Efficient Dibutyl Phthalate-Degrading Bacterium Gordonia sp. Strain QH-12.International journal of molecular sciences · 2016Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
EstS1, a newly identified thermostable esterase from Sulfobacillus acidophilus DSM10332, was heterologously expressed in Escherichia coli and shown to enzymatically degrade phthalate esters (PAEs) to their corresponding monoalkyl PAEs. The optimal pH and temperature of the esterase were found to be 8.0 and 70°C, respectively. The half-life of EstS1 at 60°C was 15 h, indicating that the enzyme had good thermostability. The specificity constant (kcat/Km) of the enzyme for p-nitrophenyl butyrate was as high as 6,770 mM(-1) s(-1). The potential value of EstS1 was demonstrated by its ability to effectively hydrolyze 35 to 82% of PAEs (10 mM) within 2 min at 37°C, with all substrates being completely degraded within 24 h. At 60°C, the time required for complete hydrolysis of most PAEs was reduced by half. To our knowledge, this enzyme is a new esterase identified from thermophiles that is able to degrade various PAEs at high temperatures.
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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.