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Updated: Aug 14, 2026
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A New Screening Method for the Directed Evolution of Thermostable Bacteriolytic Enzymes
Published on: November 7, 2012
Thermostable amylolytic enzymes from a new clostridium isolate
E Madi1, G Antranikian, K Ohmiya
1Institut für Mikrobiologie der Georg-August Universität Göttingen, 3400 Göttingen, Federal Republic of Germany, and Department of Food Science and Technology, School of Agriculture, Nagoya University, Chikusa, Nagoya 464 Japan.
Applied and Environmental Microbiology
|July 1, 1987
Summary
A novel Clostridium strain produces heat-stable alpha-amylase and pullulanase enzymes. These enzymes are induced by starch and active across a wide temperature range, showing potential for industrial applications.
Area of Science:
- Microbiology
- Enzymology
- Biochemistry
Background:
- Isolation of a novel Clostridium strain capable of starch degradation.
- Characterization of enzyme induction by various substrates.
Purpose of the Study:
- To isolate and characterize a new Clostridium strain.
- To investigate the production and properties of its amylolytic enzymes.
Main Methods:
- Isolation of Clostridium strain on starch medium at 60°C.
- Enzyme activity assays for alpha-amylase, pullulanase, and alpha-glucosidase.
- Determination of enzyme kinetics and stability.
Main Results:
- Strain produced alpha-amylase and pullulanase, induced by starch, pullulan, maltotriose, and maltose.
- Enzyme formation was growth-dependent, occurring in the exponential phase.
- Enzymes exhibited broad temperature activity (40-85°C) with optima at 60-70°C and good thermostability.
- Apparent K(m) values for starch, pullulan, and maltose were determined.
Conclusions:
- The novel Clostridium strain efficiently produces thermostable alpha-amylase and pullulanase.
- Enzyme production and localization are influenced by starch concentration.
- These enzymes demonstrate potential for biotechnological applications requiring high temperatures.
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