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Updated: Mar 11, 2026

A New Screening Method for the Directed Evolution of Thermostable Bacteriolytic Enzymes
Published on: November 7, 2012
EstDZ3: A New Esterolytic Enzyme Exhibiting Remarkable Thermostability
Dimitra Zarafeta1, Zalan Szabo2, Danai Moschidi3
1Institute of Biology, Medicinal Chemistry and Biotechnology, National Hellenic Research FoundationAthens, Greece; Laboratory of Biotechnology, School of Chemical Engineering, National Technical University of AthensAthens, Greece.
Researchers discovered EstDZ3, a highly stable lipolytic enzyme from a Chinese hot spring bacterium. This esterase maintains activity at high temperatures and in organic solvents, making it ideal for industrial applications.
Area of Science:
- Biochemistry
- Enzymology
- Biotechnology
Background:
- Lipolytic enzymes are crucial for biotechnological applications due to their catalytic activity under denaturing conditions.
- Identifying novel enzymes with high thermostability is essential for expanding their industrial utility.
Purpose of the Study:
- To discover new lipolytic enzymes resistant to prolonged exposure to elevated temperatures.
- To characterize a novel esterolytic enzyme from a hot spring microbial consortium.
Main Methods:
- Functional genomic screening of a bacterium from the genus *Dictyoglomus* isolated from a Chinese hot spring.
- Biochemical characterization of the recombinant enzyme EstDZ3.
- Computational modeling of the enzyme's three-dimensional structure.
Main Results:
- A new esterolytic enzyme, EstDZ3, was identified and characterized.
- EstDZ3 is a slightly alkalophilic esterase active against short to medium chain fatty acid esters.
- The enzyme exhibits remarkable thermostability (retaining activity up to 95°C for hours) and stability in organic solvents.
- EstDZ3 shows low similarity to known esterolytic enzymes and possesses a unique α/β hydrolase fold with a subdomain insertion.
Conclusions:
- EstDZ3 is a highly active and remarkably thermostable esterase.
- Its stability in organic solvents and unique structure make it a promising biocatalyst for high-temperature biotechnological applications.
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