Related Experiment Video
Updated: Jun 5, 2026
07:20
Bioprospecting of Extremophilic Microorganisms to Address Environmental Pollution
Published on: December 30, 2021
Mining bacterial genomes for novel arylesterase activity
Lijun Wang1, Valentina Mavisakalyan, Elisabeth R M Tillier
1Department of Chemical Engineering and Applied Chemistry, University of Toronto, 200 College Street, Toronto, ON, M5S 3E5, Canada.
Microbial Biotechnology
|January 25, 2011
Summary
Researchers screened bacterial esterases for activity, identifying several with carboxyl esterase and arylesterase functions. Highly active and stable enzymes from Rhodopseudomonas palustris and Pseudomonas putida show promise for industrial applications.
Area of Science:
- Biochemistry
- Enzymology
- Microbial Genomics
Background:
- Esterases are crucial enzymes with diverse industrial applications.
- Identifying novel esterases with specific activities and stability is an ongoing challenge.
- Bacterial genomes represent a rich source of unexplored esterase diversity.
Purpose of the Study:
- To identify and characterize novel esterases from diverse bacterial genomes.
- To evaluate the biochemical properties, including activity and stability, of selected esterases.
- To correlate sequence features with esterase activity, particularly arylesterase function.
Main Methods:
- Cloning and overexpression of 171 potential esterase genes in Escherichia coli.
- Purification and screening of 74 soluble esterase proteins for carboxyl esterase and arylesterase activity.
- Detailed biochemical characterization of selected esterases, including pH optima, thermal stability, and solvent tolerance.
Main Results:
- 36 proteins exhibited carboxyl esterase activity, and 17 showed arylesterase activity.
- Esterases from Rhodopseudomonas palustris (RpEST-1, RpEST-2, RpEST-3) and Pseudomonas putida (PpEST-1, PpEST-2, PpEST-3) were characterized.
- PpEST-3, RpEST-1, and RpEST-2 displayed high specific activity and excellent stability under various conditions, including organic solvents and ionic liquids.
- Biochemical and bioinformatic analyses provided insights into sequence features associated with arylesterase activity.
Conclusions:
- Several novel bacterial esterases with significant carboxyl esterase and arylesterase activities were identified.
- Specific esterases, notably PpEST-3, RpEST-1, and RpEST-2, demonstrate robust stability and high activity, making them promising candidates for industrial applications.
- The study facilitates the discovery of new esterases by correlating sequence data with functional properties.
Related Concept Videos
01:27Production of Antibiotics
Penicillin, one of the earliest and most widely used antibiotics, is produced industrially by the filamentous fungus Penicillium chrysogenum. Large stirred-tank bioreactors ranging from tens to hundreds of thousands of liters maintain tightly controlled temperature, pH, and dissolved oxygen conditions to support fungal metabolism and maximize antibiotic yield. Penicillin is a secondary metabolite, synthesized primarily during the stationary growth phase, which requires a carefully managed...
03:21Genome Size and the Evolution of New Genes
While every living organism has a genome of some kind (be it RNA, or DNA), there is considerable variation in the sizes of these blueprints. One major factor that impacts genome size is whether the organism is prokaryotic or eukaryotic. In prokaryotes, the genome contains little to no non-coding sequence, such that genes are tightly clustered in groups or operons sequentially along the chromosome. Conversely, the genes in eukaryotes are punctuated by long stretches of non-coding sequence.