ArticleBiotechnology letters2013
Heterologous expression and characterization of a malathion-hydrolyzing carboxylesterase from a thermophilic bacterium, Alicyclobacillus tengchongensis.
Article in Biotechnology letters, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 31 citations in OpenAlex.
- Malathion biodegradation and biotransformation in water and sediment systems: bacterial pathways, environmental drivers, ecological impacts, and bioremediation strategies.World journal of microbiology & biotechnology · 2026Review
- Environmental Adaptability and Organic Pollutant Degradation Capacity of a NovelMicroorganisms · 2022Article
- Presence of esterase and laccase in Bacillus subtilis facilitates biodegradation and detoxification of cypermethrin.Scientific reports · 2018Article
- Functional Analysis of a Carboxylesterase Gene Associated With Isoprocarb and Cyhalothrin Resistance inFrontiers in physiology · 2018Article
- New Insights into the Microbiota of Moth Pests.International journal of molecular sciences · 2017Review
- Identification and Characterization of a New 7-Aminocephalosporanic Acid Deacetylase from Thermophilic Bacterium Alicyclobacillus tengchongensis.Journal of bacteriology · 2016Article
- Functional Analysis of Esterase TCE2 Gene from Tetranychus cinnabarinus (Boisduval) involved in Acaricide Resistance.Scientific reports · 2016Article
- Detection of carboxylesterase and esterase activity in culturable gut bacterial flora isolated from diamondback moth, Plutella xylostella (Linnaeus), from India and its possible role in indoxacarb degradation.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology]Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A carboxylesterase gene from thermophilic bacterium, Alicyclobacillus tengchongensis, was cloned and expressed in Escherichia coli BL21 (DE3). The gene coded for a 513 amino acid protein with a calculated molecular mass of 57.82 kDa. The deduced amino acid sequence had structural features highly conserved among serine hydrolases, including Ser204, Glu325, and His415 as a catalytic triad, as well as type-B carboxylesterase serine active site (FGGDPENITIGGQSAG) and type-B carboxylesterase signature 2 (EDCLYLNIWTP). The purified enzyme exhibited optimum activity with β-naphthyl acetate at 60 °C and pH 7 as well as stability at 25 °C and pH 7. One unit of the enzyme hydrolyzed 5 mg malathion l(-1) by 50 % within 25 min and 89 % within 100 min. The enzyme strongly degraded malathion and has a potential use for the detoxification of malathion residues.
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