ArticleExtremophiles : life under extreme conditions2016
Biochemical characterization and structural analysis of a new cold-active and salt-tolerant esterase from the marine bacterium Thalassospira sp.
Article in Extremophiles : life under extreme conditions, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed.
- Article
- Expression and characterization of a Clostridium Butyricum esterase from pit cellar of Chinese liquor and its potential in flavor ester synthesis.Archives of microbiology · 2025Article
- C-Terminal β8-α9 Interaction Modulates Thermal Stability and Enzymatic Activity Differently in Hyperthermophilic Esterase EstE1 and Mesophilic Esterase rPPE.Applied and environmental microbiology · 2023Article
- N-terminal lid swapping contributes to the substrate specificity and activity of thermophilic lipase TrLipE.Frontiers in microbiology · 2023Article
- Crystal structure and biochemical analysis of acetylesterase (LgEstI) from Lactococcus garvieae.PloS one · 2023Article
- Marine Bioprospecting, Biocatalysis and Process Development.Microorganisms · 2022Review
- Regulated strategies of cold-adapted microorganisms in response to cold: a review.Environmental science and pollution research international · 2021Review
- Structure andOpen biology · 2021Article
- Thalassobacillus, a genus of extreme to moderate environmental halophiles with biotechnological potential.World journal of microbiology & biotechnology · 2021Review
- Marine Bacterial Esterases: Emerging Biocatalysts for Industrial Applications.Applied biochemistry and biotechnology · 2021Review
- Article
- Characterization of a novel halotolerant esterase from3 Biotech · 2020Article
- Extremophile Microbial Communities and Enzymes for Bioenergetic Application Based on Multi-Omics Tools.Current genomics · 2020Review
- Molecular and Biochemical Characterization of Salt-Tolerant Trehalose-6-Phosphate Hydrolases Identified by Screening and Sequencing Salt-Tolerant Clones From the Metagenomic Library of the Gastrointestinal Tract.Frontiers in microbiology · 2020Article
- Enzymes from Marine Polar Regions and Their Biotechnological Applications.Marine drugs · 2019Review
- Structural and Functional Insights Into CmGH1, a Novel GH39 Family β-Glucosidase From Deep-Sea Bacterium.Frontiers in microbiology · 2019Article
- Cold active pectinase, amylase and protease production by yeast isolates obtained from environmental samples.Extremophiles : life under extreme conditions · 2018Article
- Functional characterization of hormone sensitive-like lipase from Bacillus halodurans: synthesis and recovery of pNP-laurate with high yields.Extremophiles : life under extreme conditions · 2017Article
- A family of archaea-like carboxylesterases preferentially expressed in the symbiotic phase of the mychorrizal fungus Tuber melanosporum.Scientific reports · 2017Article
- Crystal Structure and Functional Characterization of an Esterase (EaEST) from Exiguobacterium antarcticum.PloS one · 2017Article
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Authors and funding
6 authors.
Funding
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Abstract
A gene encoding an esterase, ThaEst2349, was identified in the marine psychrophilic bacterium Thalassospira sp. GB04J01. The gene was cloned and overexpressed in E. coli as a His-tagged fusion protein. The recombinant enzyme showed optimal activity at 45 °C and the thermal stability displayed a retention of 75 % relative activity at 40 °C after 2 h. The optimal pH was 8.5 but the enzyme kept more than 75 % of its maximal activity between pH 8.0 and 9.5. ThaEst2349 also showed remarkable tolerance towards high concentrations of salt and it was active against short-chain p-nitrophenyl esters, displaying optimal activity with the acetate. The enzyme was tested for tolerance of organic solvents and the results are suggesting that it could function as an interesting candidate for biotechnological applications. The crystal structure of ThaEst2349 was determined to 1.69 Å revealing an asymmetric unit containing two chains, which also is the biological unit. The structure has a characteristic cap domain and a catalytic triad comprising Ser158, His285 and Asp255. To explain the cold-active nature of the enzyme, we compared it against thermophilic counterparts. Our hypothesis is that a high methionine content, less hydrogen bonds and less ion pairs render the enzyme more flexible at low temperatures.
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