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Characterization of esterase activity in Geobacillus sp. HBB-4
Kubilay Metin1, Z Burcu Bakir Ateslier, Gamze Basbulbul
1Department of Biology, Faculty of Science and Literature, Adnan Menderes University, 09010 Aydin, Turkey. kmetin@adu.edu.tr
Journal of Basic Microbiology
|September 30, 2006
Summary
A novel thermophilic esterase from Geobacillus sp. HBB-4, isolated from a Turkish thermal spring, shows enhanced activity with specific metal ions and detergents. Its thermostability suggests potential for industrial applications.
Area of Science:
- Microbiology
- Enzymology
- Biochemistry
Background:
- A thermophilic bacterium, Bacillus sp. 4, was isolated from a thermal spring in Turkey.
- The bacterium was identified as Geobacillus sp. HBB-4 using 16S rRNA gene sequencing.
- Geobacillus sp. HBB-4 is closely related to Bacillus sp. BGSC W9A59, belonging to the newly described Geobacillus genus.
Purpose of the Study:
- To characterize the effects of various chemicals on the activity of a thermostable esterase from Geobacillus sp. HBB-4.
- To evaluate the potential industrial applications of this enzyme.
Main Methods:
- Bacterial identification using 16S rRNA gene sequencing.
- Enzyme activity assays were performed under various chemical conditions (metal ions, detergents, organic solvents).
Main Results:
- Esterase activity was enhanced by manganese (Mn+2) and nickel (Ni+2) ions.
- Activity was inhibited by mercury (Hg+2) and copper (Cu+2) ions; calcium (Ca+2), magnesium (Mg+2), and cobalt (Co+2) had no effect.
- Ionic detergents inhibited activity, while non-ionic detergents and dimethyl sulfoxide (DMSO) activated it. Ethanol and methanol maintained over 50% activity.
Conclusions:
- Geobacillus sp. HBB-4 esterase exhibits significant thermostability and unique responses to various chemical agents.
- The enzyme's characteristics, including activation by specific metal ions and detergents, indicate its potential for diverse industrial applications.
